BrabA.11339.a: anomalous diffraction and ligand binding guide towards the elucidation of the function of a `putative β-lactamase-like protein' from Brucella melitensis

Abendroth, Jan; Sankaran, Banumathi; Edwards, Thomas E.; Gardberg, Anna S.; Dieterich, Shellie; Bhandari, Janhavi; Napuli, Alberto J.; Van Voorhis, Wesley C.; Staker, Bart L.; Myler, Peter J.; Stewart, Lance J.

doi:10.1107/s1744309111010220

Title: BrabA.11339.a: anomalous diffraction and ligand binding guide towards the elucidation of the function of a `putative β-lactamase-like protein' from Brucella melitensis

Journal Article · Tue Aug 16 00:00:00 EDT 2011 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/s1744309111010220· OSTI ID:1625808

Abendroth, Jan ^[1]; Sankaran, Banumathi ^[2]; Edwards, Thomas E. ^[3]; Gardberg, Anna S. ^[3]; Dieterich, Shellie ^[3]; Bhandari, Janhavi ^[4]; Napuli, Alberto J. ^[4]; Van Voorhis, Wesley C. ^[4]; Staker, Bart L. ^[3]; Myler, Peter J. ^[5]; Stewart, Lance J. ^[3]

Seattle Structural Genomics Center for Infectious Disease (SSGCID), Seattle, WA (United States); Emerald BioStructures Inc., Bainbridge Island, WA (United States)
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States). Berkeley Center for Structural Biology
Seattle Structural Genomics Center for Infectious Disease (SSGCID), Seattle, WA (United States); Emerald BioStructures Inc., Bainbridge Island, WA (United States)
Seattle Structural Genomics Center for Infectious Disease (SSGCID), Seattle, WA (United States); Univ. of Washington, Seattle, WA (United States). School of Medicine. Dept. of Allergy and Infectious Diseases
Seattle Structural Genomics Center for Infectious Disease (SSGCID), Seattle, WA (United States); Seattle Biomedical Research Inst., Seattle, WA (United States)

The crystal structure of a -lactamase-like protein from Brucella melitensis was initially solved by SAD phasing from an in-house data set collected on a crystal soaked with iodide. A high-resolution data set was collected at a synchroton at the Se edge wavelength, which also provided an independent source of phasing using a small anomalous signal from metal ions in the active site. Comparisons of anomalous peak heights at various wavelengths allowed the identification of the active-site metal ions as manganese. In the native data set a partially occupied GMP could be identified. When co-crystallized with AMPPNP or GMPPNP, clear density for the hydrolyzed analogs was observed, providing hints to the function of the protein.

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Research Organization:: Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Biological and Environmental Research (BER). Biological Systems Science Division

Grant/Contract Number:: AC02-05CH11231

OSTI ID:: 1625808

Journal Information:: Acta Crystallographica. Section F, Vol. 67, Issue 9; ISSN 1744-3091

Publisher:: International Union of CrystallographyCopyright Statement

Country of Publication:: United States

Language:: English

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Dual Specificity and Novel Structural Folding of Yeast Phosphodiesterase-1 for Hydrolysis of Second Messengers Cyclic Adenosine and Guanosine 3′,5′-Monophosphate Tian, Yuanyuan; Cui, Wenjun; Huang, Manna Biochemistry, Vol. 53, Issue 30 https://doi.org/10.1021/bi500406h	journal	July 2014

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Title: BrabA.11339.a: anomalous diffraction and ligand binding guide towards the elucidation of the function of a `putative β-lactamase-like protein' from Brucella melitensis

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