A High-Resolution Crystal Structure of a Psychrohalophilic α–Carbonic Anhydrase from Photobacterium profundum Reveals a Unique Dimer Interface

Somalinga, Vijayakumar; Buhrman, Greg; Arun, Ashikha; Rose, Robert B.; Grunden, Amy M.; Hofmann, Andreas

doi:10.1371/journal.pone.0168022

Title: A High-Resolution Crystal Structure of a Psychrohalophilic α–Carbonic Anhydrase from Photobacterium profundum Reveals a Unique Dimer Interface

Journal Article · Fri Dec 09 00:00:00 EST 2016 · PLoS ONE

DOI:https://doi.org/10.1371/journal.pone.0168022· OSTI ID:1335983

Somalinga, Vijayakumar ^[1]; Buhrman, Greg ^[1]; Arun, Ashikha ^[1]; Rose, Robert B. ^[1];

^[1]; Hofmann, Andreas ^[2]

North Carolina State Univ., Raleigh, NC (United States)
Griffith Univ. (Australia)

Bacterial α–carbonic anhydrases (α-CA) are zinc containing metalloenzymes that catalyze the rapid interconversion of CO₂ to bicarbonate and a proton. We report the first crystal structure of a pyschrohalophilic α–CA from a deep-sea bacterium, Photobacterium profundum. Size exclusion chromatography of the purified P. profundum α–CA (PprCA) reveals that the protein is a heterogeneous mix of monomers and dimers. Furthermore, an “in-gel” carbonic anhydrase activity assay, also known as protonography, revealed two distinct bands corresponding to monomeric and dimeric forms of PprCA that are catalytically active. The crystal structure of PprCA was determined in its native form and reveals a highly conserved “knot-topology” that is characteristic of α–CA’s. Similar to other bacterial α–CA’s, PprCA also crystallized as a dimer. Furthermore, dimer interface analysis revealed the presence of a chloride ion (Cl-) in the interface which is unique to PprCA and has not been observed in any other α–CA’s characterized so far. Molecular dynamics simulation and chloride ion occupancy analysis shows 100% occupancy for the Cl- ion in the dimer interface. Zinc coordinating triple histidine residues, substrate binding hydrophobic patch residues, and the hydrophilic proton wire residues are highly conserved in PprCA and are identical to other well-studied α–CA’s.

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Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States)

Sponsoring Organization:: USDOE

OSTI ID:: 1335983

Journal Information:: PLoS ONE, Vol. 11, Issue 12; ISSN 1932-6203

Publisher:: Public Library of ScienceCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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Cited by: 10 works

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Crystal Structure of a Highly Thermostable α-Carbonic Anhydrase from Persephonella marina EX-H1 Kim, Subin; Sung, Jongmin; Yeon, Jungyoon Molecules and Cells, Vol. 42, Issue 6 https://doi.org/10.14348/molcells.2019.0029	journal	June 2019
Mechanism of Action of Non-Synonymous Single Nucleotide Variations Associated with α-Carbonic Anhydrase II Deficiency Sanyanga, Taremekedzwa Allan; Nizami, Bilal; Bishop, Özlem Tastan Molecules, Vol. 24, Issue 21 https://doi.org/10.3390/molecules24213987	journal	November 2019

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Title: A High-Resolution Crystal Structure of a Psychrohalophilic α–Carbonic Anhydrase from Photobacterium profundum Reveals a Unique Dimer Interface

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