6im3: Difference between revisions

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New page: '''Unreleased structure''' The entry 6im3 is ON HOLD Authors: Jin, M.S., Kim, S., Sung, J., Yeon, J., Choi, S.H. Description: Crystal structure of a highly thermostable carbonic anhydr...
 
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'''Unreleased structure'''


The entry 6im3 is ON HOLD
==Crystal structure of a highly thermostable carbonic anhydrase from Persephonella marina EX-H1==
<StructureSection load='6im3' size='340' side='right'caption='[[6im3]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6im3]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Persephonella_marina_EX-H1 Persephonella marina EX-H1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IM3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IM3 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AZM:5-ACETAMIDO-1,3,4-THIADIAZOLE-2-SULFONAMIDE'>AZM</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6im3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6im3 OCA], [https://pdbe.org/6im3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6im3 RCSB], [https://www.ebi.ac.uk/pdbsum/6im3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6im3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/C0QRB5_PERMH C0QRB5_PERMH]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacterial alpha-type carbonic anhydrase (alpha-CA) is a zinc metalloenzyme that catalyzes the reversible and extremely rapid interconversion of carbon dioxide to bicarbonate. In this study, we report the first crystal structure of a hyperthermostable alpha-CA from Persephonella marina EXH1 (pm CA) in the absence and presence of competitive inhibitor, acetazolamide. The structure reveals a compactly folded pm CA homodimer in which each monomer consists of a 10-stranded beta-sheet in the center. The catalytic zinc ion is coordinated by three highly conserved histidine residues with an exchangeable fourth ligand (a water molecule, a bicarbonate anion, or the sulfonamide group of acetazolamide). Together with an intramolecular disulfide bond, extensive interfacial networks of hydrogen bonds, ionic and hydrophobic interactions stabilize the dimeric structure and are likely responsible for the high thermal stability. We also identified novel binding sites for calcium ions at the crystallographic interface, which serve as molecular glue linking negatively charged and otherwise repulsive surfaces. Furthermore, this large negatively charged patch appears to further increase the thermostability at alkaline pH range via favorable charge-charge interactions between pm CA and solvent molecules. These findings may assist development of novel alpha-CAs with improved thermal and/or alkaline stability for applications such as CO2 capture and sequestration.


Authors: Jin, M.S., Kim, S., Sung, J., Yeon, J., Choi, S.H.
Crystal Structure of a Highly Thermostable alpha-Carbonic Anhydrase from Persephonella marina EX-H1.,Kim S, Sung J, Yeon J, Choi SH, Jin MS Mol Cells. 2019 Jun 30;42(6):460-469. doi: 10.14348/molcells.2019.0029. PMID:31250619<ref>PMID:31250619</ref>


Description: Crystal structure of a highly thermostable carbonic anhydrase from Persephonella marina EX-H1
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Choi, S.H]]
<div class="pdbe-citations 6im3" style="background-color:#fffaf0;"></div>
[[Category: Yeon, J]]
 
[[Category: Sung, J]]
==See Also==
[[Category: Kim, S]]
*[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]]
[[Category: Jin, M.S]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Persephonella marina EX-H1]]
[[Category: Choi SH]]
[[Category: Jin MS]]
[[Category: Kim S]]
[[Category: Sung J]]
[[Category: Yeon J]]

Latest revision as of 12:45, 22 November 2023

Crystal structure of a highly thermostable carbonic anhydrase from Persephonella marina EX-H1Crystal structure of a highly thermostable carbonic anhydrase from Persephonella marina EX-H1

Structural highlights

6im3 is a 6 chain structure with sequence from Persephonella marina EX-H1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

C0QRB5_PERMH

Publication Abstract from PubMed

Bacterial alpha-type carbonic anhydrase (alpha-CA) is a zinc metalloenzyme that catalyzes the reversible and extremely rapid interconversion of carbon dioxide to bicarbonate. In this study, we report the first crystal structure of a hyperthermostable alpha-CA from Persephonella marina EXH1 (pm CA) in the absence and presence of competitive inhibitor, acetazolamide. The structure reveals a compactly folded pm CA homodimer in which each monomer consists of a 10-stranded beta-sheet in the center. The catalytic zinc ion is coordinated by three highly conserved histidine residues with an exchangeable fourth ligand (a water molecule, a bicarbonate anion, or the sulfonamide group of acetazolamide). Together with an intramolecular disulfide bond, extensive interfacial networks of hydrogen bonds, ionic and hydrophobic interactions stabilize the dimeric structure and are likely responsible for the high thermal stability. We also identified novel binding sites for calcium ions at the crystallographic interface, which serve as molecular glue linking negatively charged and otherwise repulsive surfaces. Furthermore, this large negatively charged patch appears to further increase the thermostability at alkaline pH range via favorable charge-charge interactions between pm CA and solvent molecules. These findings may assist development of novel alpha-CAs with improved thermal and/or alkaline stability for applications such as CO2 capture and sequestration.

Crystal Structure of a Highly Thermostable alpha-Carbonic Anhydrase from Persephonella marina EX-H1.,Kim S, Sung J, Yeon J, Choi SH, Jin MS Mol Cells. 2019 Jun 30;42(6):460-469. doi: 10.14348/molcells.2019.0029. PMID:31250619[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Kim S, Sung J, Yeon J, Choi SH, Jin MS. Crystal Structure of a Highly Thermostable alpha-Carbonic Anhydrase from Persephonella marina EX-H1. Mol Cells. 2019 Jun 30;42(6):460-469. doi: 10.14348/molcells.2019.0029. PMID:31250619 doi:http://dx.doi.org/10.14348/molcells.2019.0029

6im3, resolution 2.00Å

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