3oup: Difference between revisions

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<StructureSection load='3oup' size='340' side='right'caption='[[3oup]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
<StructureSection load='3oup' size='340' side='right'caption='[[3oup]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3oup]] 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=3OUP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OUP FirstGlance]. <br>
<table><tr><td colspan='2'>[[3oup]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanosarcina_thermophila Methanosarcina thermophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OUP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OUP FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3otm|3otm]], [[3otz|3otz]], [[3ou9|3ou9]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] </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=3oup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oup OCA], [https://pdbe.org/3oup PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oup RCSB], [https://www.ebi.ac.uk/pdbsum/3oup PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oup 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=3oup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oup OCA], [https://pdbe.org/3oup PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oup RCSB], [https://www.ebi.ac.uk/pdbsum/3oup PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oup ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://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_METTT CAH_METTT] Reversible hydration of carbon dioxide. Important for growth on acetate (PubMed:8041719). As a probably extracellular enzyme, it may support a H(+)/CH(3)COO(-) symport mechanism and/or conversion of CO(2) to HCO(3)(-), removing excess CO(2) produced by growth on acetate (Probable).<ref>PMID:8041719</ref> <ref>PMID:10924115</ref> <ref>PMID:8041719</ref> <ref>PMID:8665839</ref>


==See Also==
==See Also==
*[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]]
*[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Carbonate dehydratase]]
[[Category: Dsm 1825]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Domsic, J F]]
[[Category: Methanosarcina thermophila]]
[[Category: McKenna, R]]
[[Category: Domsic JF]]
[[Category: Robbins, A H]]
[[Category: McKenna R]]
[[Category: Left-handed beta helix]]
[[Category: Robbins AH]]
[[Category: Ligands to zinc]]
[[Category: Lyase]]
[[Category: Trimer]]

Latest revision as of 13:36, 21 February 2024

Crystal structure of the gamma-carbonic anhydrase W19N mutant from Methanosarcina thermophilaCrystal structure of the gamma-carbonic anhydrase W19N mutant from Methanosarcina thermophila

Structural highlights

3oup is a 1 chain structure with sequence from Methanosarcina thermophila. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.65Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CAH_METTT Reversible hydration of carbon dioxide. Important for growth on acetate (PubMed:8041719). As a probably extracellular enzyme, it may support a H(+)/CH(3)COO(-) symport mechanism and/or conversion of CO(2) to HCO(3)(-), removing excess CO(2) produced by growth on acetate (Probable).[1] [2] [3] [4]

See Also

References

  1. ↑ Alber BE, Ferry JG. A carbonic anhydrase from the archaeon Methanosarcina thermophila. Proc Natl Acad Sci U S A. 1994 Jul 19;91(15):6909-13. PMID:8041719
  2. ↑ 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
  3. ↑ Alber BE, Ferry JG. A carbonic anhydrase from the archaeon Methanosarcina thermophila. Proc Natl Acad Sci U S A. 1994 Jul 19;91(15):6909-13. PMID:8041719
  4. ↑ Kisker C, Schindelin H, Alber BE, Ferry JG, Rees DC. A left-hand beta-helix revealed by the crystal structure of a carbonic anhydrase from the archaeon Methanosarcina thermophila. EMBO J. 1996 May 15;15(10):2323-30. PMID:8665839

3oup, resolution 1.65Å

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