Bacterial Pleckstrin Homology Domains: a Prokaryotic Origin for the Ph Domain

Xu, Q.; Bateman, A.; Finn, R. D.; Abdubek, P.; Astakhova, T.; Axelrod, H. L.; Bakolitsa, C.; Carlton, D.; Chen, C.; Chiu, H. -J.; Chiu, M.; Clayton, T.; Das, D.; Deller, M. C.; Duan, L.; Ellrott, K.; Ernst, D.; Farr, C. L.; Feuerhelm, J.; Grant, J. C.; Grzechnik, A.

Title: Bacterial Pleckstrin Homology Domains: a Prokaryotic Origin for the Ph Domain

Full Record
Other Related Research

Authors:: Xu, Q.; Bateman, A.; Finn, R. D.; Abdubek, P.; Astakhova, T.; Axelrod, H. L.; Bakolitsa, C.; Carlton, D.; Chen, C.; Chiu, H. -J.; Chiu, M.; Clayton, T.; Das, D.; Deller, M. C.; Duan, L.; Ellrott, K.; Ernst, D.; Farr, C. L.; Feuerhelm, J.; Grant, J. C. more »« less

Publication Date:: Tue Jul 30 00:00:00 EDT 2013

Research Org.:: SLAC National Accelerator Lab., Menlo Park, CA (United States)

Sponsoring Org.:: USDOE Office of Science (SC)

OSTI Identifier:: 1089199

Report Number(s):: SLAC-REPRINT-2013-320

DOE Contract Number:: AC02-76SF00515

Resource Type:: Journal Article

Journal Name:: J. Mol. Biol 396:31,2010

Additional Journal Information:: Journal Name: J. Mol. Biol 396:31,2010

Country of Publication:: United States

Language:: English

Subject:: BIO

Citation Formats


                    Xu, Q., Bateman, A., Finn, R. D., Abdubek, P., Astakhova, T., Axelrod, H. L., Bakolitsa, C., Carlton, D., Chen, C., Chiu, H. -J., Chiu, M., Clayton, T., Das, D., Deller, M. C., Duan, L., Ellrott, K., Ernst, D., Farr, C. L., Feuerhelm, J., Grant, J. C., Grzechnik, A., and /SLAC. Bacterial Pleckstrin Homology Domains: a Prokaryotic Origin for the Ph Domain.  United States: N. p., 2013. 
        Web.

Copy to clipboard


                    Xu, Q., Bateman, A., Finn, R. D., Abdubek, P., Astakhova, T., Axelrod, H. L., Bakolitsa, C., Carlton, D., Chen, C., Chiu, H. -J., Chiu, M., Clayton, T., Das, D., Deller, M. C., Duan, L., Ellrott, K., Ernst, D., Farr, C. L., Feuerhelm, J., Grant, J. C., Grzechnik, A., & /SLAC. Bacterial Pleckstrin Homology Domains: a Prokaryotic Origin for the Ph Domain.  United States.

Copy to clipboard


                    Xu, Q., Bateman, A., Finn, R. D., Abdubek, P., Astakhova, T., Axelrod, H. L., Bakolitsa, C., Carlton, D., Chen, C., Chiu, H. -J., Chiu, M., Clayton, T., Das, D., Deller, M. C., Duan, L., Ellrott, K., Ernst, D., Farr, C. L., Feuerhelm, J., Grant, J. C., Grzechnik, A., and /SLAC. 2013.  
        "Bacterial Pleckstrin Homology Domains: a Prokaryotic Origin for the Ph Domain".  United States.

Copy to clipboard


                    
@article{osti_1089199,

  title        = {Bacterial Pleckstrin Homology Domains: a Prokaryotic Origin for the Ph Domain},

  author       = {Xu, Q. and Bateman, A. and Finn, R. D. and Abdubek, P. and Astakhova, T. and Axelrod, H. L. and Bakolitsa, C. and Carlton, D. and Chen, C. and Chiu, H. -J. and Chiu, M. and Clayton, T. and Das, D. and Deller, M. C. and Duan, L. and Ellrott, K. and Ernst, D. and Farr, C. L. and Feuerhelm, J. and Grant, J. C. and Grzechnik, A. and /SLAC},

  abstractNote = {},

  doi          = {},

  url          = {https://www.osti.gov/biblio/1089199},
  journal      = {J. Mol. Biol 396:31,2010},
number       = ,

  volume       = ,

  place        = {United States},

  year         = {Tue Jul 30 00:00:00 EDT 2013},

  month        = {Tue Jul 30 00:00:00 EDT 2013}

}

Copy to clipboard

Journal Article:

Other availability

Find in Google Scholar

Search WorldCat to find libraries that may hold this journal

Save / Share:

Export Metadata

Save to My Library

Similar records in OSTI.GOV collections:

Bacterial Pleckstrin Homology Domains: A Prokaryotic Origin for the PH Domain

Journal Article Xu, Qingping; Bateman, Alex; Finn, Robert; ... - Journal of Molecular Biology

Pleckstrin homology (PH) domains have been identified only in eukaryoticproteins to date. We have determined crystal structures for three membersof an uncharacterized protein family (Pfam PF08000), which providecompelling evidence for the existence of PH-like domains in bacteria (PHb).The first two structures contain a single PHbdomain that forms a dome-shaped, oligomeric ring with C5symmetry. The third structure has anadditional helical hairpin attached at the C-terminus and forms a similar butmuch larger ring with C12symmetry. Thus, both molecular assembliesexhibit rare, higher-order, cyclic symmetry but preserve a similararrangement of their PHbdomains, which gives rise to a conservedhydrophilic surface at the intersection of theβ-strandsmore »« less
Cited by 25
https://doi.org/10.1016/j.jmb.2009.11.006
Molecular Basis of Phosphatidylinositol 4-Phosphate and ARF1 GTPase Recognition by the FAPP1 Pleckstrin Homology (PH) Domain

Journal Article He, J; Heroux, A; Scott, J; ... - Journal of Biological Chemistry

Four-phosphate-adaptor protein 1 (FAPP1) regulates secretory transport from the trans-Golgi network (TGN) to the plasma membrane. FAPP1 is recruited to the Golgi through binding of its pleckstrin homology (PH) domain to phosphatidylinositol 4-phosphate (PtdIns(4)P) and a small GTPase ADP-ribosylation factor 1 (ARF1). Despite the critical role of FAPP1 in membrane trafficking, the molecular basis of its dual function remains unclear. Here, we report a 1.9 {angstrom} resolution crystal structure of the FAPP1 PH domain and detail the molecular mechanisms of the PtdIns(4)P and ARF1 recognition. The FAPP1 PH domain folds into a seven-stranded {beta}-barrel capped by an {alpha}-helix at onemore »« less
https://doi.org/10.1074/jbc.M111.233015
Activated RhoA Binds to the Pleckstrin Homology (PH) Domain of PDZ-RhoGEF, a Potential Site for Autoregulation

Journal Article Chen, Zhe; Medina, Frank; Liu, Mu-ya; ... - J. Biol. Chem.

Guanine nucleotide exchange factors (GEFs) catalyze exchange of GDP for GTP by stabilizing the nucleotide-free state of the small GTPases through their Dbl homology/pleckstrin homology (DH {center_dot} PH) domains. Unconventionally, PDZ-RhoGEF (PRG), a member of the RGS-RhoGEFs, binds tightly to both nucleotide-free and activated RhoA (RhoA {center_dot} GTP). We have characterized the interaction between PRG and activated RhoA and determined the structure of the PRG-DH {center_dot} PH-RhoA {center_dot} GTP{gamma}S (guanosine 5{prime}-O-[{gamma}-thio]triphosphate) complex. The interface bears striking similarity to a GTPase-effector interface and involves the switch regions in RhoA and a hydrophobic patch in PRG-PH that is conserved among all Lbcmore »« less
https://doi.org/10.1074/jbc.M110.122549
The Tiam1 guanine nucleotide exchange factor is auto-inhibited by its pleckstrin homology coiled-coil extension domain

Journal Article Xu, Zhen; Gakhar, Lokesh; Bain, Fletcher; ... - Journal of Biological Chemistry

T-cell lymphoma invasion and metastasis 1 (Tiam1) is a Dbl-family guanine nucleotide exchange factor (GEF) that specifically activates the Rho-family GTPase Rac1 in response to upstream signals, thereby regulating cellular processes including cell adhesion and migration. Tiam1 contains multiple domains, including an N-terminal pleckstrin homology coiled-coiled extension (PH_n-CC-Ex) and catalytic Dbl homology and C-terminal pleckstrin homology (DH-PH_c) domain. Previous studies indicate that larger fragments of Tiam1, such as the region encompassing the N-terminal to C-terminal pleckstrin homology domains (PH_n-PH_c), are auto-inhibited. However, the domains in this region responsible for inhibition remain unknown. Here, we show that the PH_n-CC-Ex domain inhibitsmore »« less
Cited by 9
https://doi.org/10.1074/jbc.M117.799114

Full Text Available
Structural and Functional Studies of the Ras-Associating and Pleckstrin Homology Domains of Grb10 and Grb14

Journal Article Depetris, R; Wu, J; Hubbard, S - Nature Structural and Molecular Biology

Growth factor receptor-binding proteins Grb7, Grb10 and Grb14 are adaptor proteins containing a Ras-associating (RA) domain, a pleckstrin-homology (PH) domain, a family-specific BPS (between PH and SH2) region and a C-terminal Src-homology-2 domain. Previous structural studies showed that the Grb14 BPS region binds as a pseudosubstrate inhibitor in the tyrosine kinase domain of the insulin receptor to suppress insulin signaling. Here we report the crystal structure of the RA and PH domains of Grb10 at 2.6-A resolution. The structure reveals that these two domains, along with the intervening linker, form an integrated, dimeric structural unit. Biochemical studies demonstrated that Grb14more »« less
https://doi.org/10.1038/nsmb1209-1331a

Similar Records