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1qre

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Revision as of 10:02, 15 September 2021

A CLOSER LOOK AT THE ACTIVE SITE OF GAMMA-CARBONIC ANHYDRASES: HIGH RESOLUTION CRYSTALLOGRAPHIC STUDIES OF THE CARBONIC ANHYDRASE FROM METHANOSARCINA THERMOPHILA

Structural highlights

1qre is a 1 chain structure with sequence from Dsm 1825. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1thj, 1qq0, 1qrf, 1qrg, 1qrl, 1qrm
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CAH_METTE] Reversible hydration of carbon dioxide. Essential to photosynthetic carbon dioxide fixation.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The prototype of the gamma-class of carbonic anhydrase has been characterized from the methanogenic archaeon Methanosarcina thermophila. Previously reported kinetic studies of the gamma-class carbonic anhydrase are consistent with this enzyme having a reaction mechanism similar to that of the mammalian alpha-class carbonic anhydrase. However, the overall folds of these two enzymes are dissimilar, and apart from the zinc-coordinating histidines, the active site residues bear little resemblance to one another. The crystal structures of zinc-containing and cobalt-substituted gamma-class carbonic anhydrases from M. thermophila are reported here between 1.46 and 1.95 A resolution in the unbound form and cocrystallized with either SO(4)(2)(-) or HCO(3)(-). Relative to the tetrahedral coordination geometry seen at the active site in the alpha-class of carbonic anhydrases, the active site of the gamma-class enzyme contains additional metal-bound water ligands, so the overall coordination geometry is trigonal bipyramidal for the zinc-containing enzyme and octahedral for the cobalt-substituted enzyme. Ligands bound to the active site all make contacts with the side chain of Glu 62 in manners that suggest the side chain is likely protonated. In the uncomplexed zinc-containing enzyme, the side chains of Glu 62 and Glu 84 appear to share a proton; additionally, Glu 84 exhibits multiple conformations. This suggests that Glu 84 may act as a proton shuttle, which is an important aspect of the reaction mechanism of alpha-class carbonic anhydrases. A hydrophobic pocket on the surface of the enzyme may participate in the trapping of CO(2) at the active site. On the basis of the coordination geometry at the active site, ligand binding modes, the behavior of the side chains of Glu 62 and Glu 84, and analogies to the well-characterized alpha-class of carbonic anhydrases, a more-defined reaction mechanism is proposed for the gamma-class of carbonic anhydrases.

A closer look at the active site of gamma-class carbonic anhydrases: high-resolution crystallographic studies of the carbonic anhydrase from Methanosarcina thermophila.,Iverson TM, Alber BE, Kisker C, Ferry JG, Rees DC Biochemistry. 2000 Aug 8;39(31):9222-31. PMID:10924115^[1]

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

References

↑ Iverson TM, Alber BE, Kisker C, Ferry JG, Rees DC. A closer look at the active site of gamma-class carbonic anhydrases: high-resolution crystallographic studies of the carbonic anhydrase from Methanosarcina thermophila. Biochemistry. 2000 Aug 8;39(31):9222-31. PMID:10924115

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1qre"

@@ Line 3: / Line 3: @@
 <StructureSection load='1qre' size='340' side='right'caption='[[1qre]], [[Resolution|resolution]] 1.46&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1qre]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Dsm_1825 Dsm 1825]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QRE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QRE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1qre]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Dsm_1825 Dsm 1825]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QRE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QRE FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BCT:BICARBONATE+ION'>BCT</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCT:BICARBONATE+ION'>BCT</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1thj|1thj]], [[1qq0|1qq0]], [[1qrf|1qrf]], [[1qrg|1qrg]], [[1qrl|1qrl]], [[1qrm|1qrm]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1thj|1thj]], [[1qq0|1qq0]], [[1qrf|1qrf]], [[1qrg|1qrg]], [[1qrl|1qrl]], [[1qrm|1qrm]]</div></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qre OCA], [http://pdbe.org/1qre PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qre RCSB], [http://www.ebi.ac.uk/pdbsum/1qre PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qre ProSAT]</span></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=1qre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qre OCA], [https://pdbe.org/1qre PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qre RCSB], [https://www.ebi.ac.uk/pdbsum/1qre PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qre ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CAH_METTE CAH_METTE]] Reversible hydration of carbon dioxide. Essential to photosynthetic carbon dioxide fixation.
+[[https://www.uniprot.org/uniprot/CAH_METTE CAH_METTE]] Reversible hydration of carbon dioxide. Essential to photosynthetic carbon dioxide fixation.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 32: @@
 ==See Also==
 *[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]]
-*[[Gamma Carbonic Anhydrase|Gamma Carbonic Anhydrase]]
 == References ==
 <references/>

1qre

From Proteopedia

Revision as of 10:02, 15 September 2021

A CLOSER LOOK AT THE ACTIVE SITE OF GAMMA-CARBONIC ANHYDRASES: HIGH RESOLUTION CRYSTALLOGRAPHIC STUDIES OF THE CARBONIC ANHYDRASE FROM METHANOSARCINA THERMOPHILA

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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