1jzk: Difference between revisions
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<StructureSection load='1jzk' size='340' side='right'caption='[[1jzk]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='1jzk' size='340' side='right'caption='[[1jzk]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1jzk]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JZK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JZK FirstGlance]. <br> | <table><tr><td colspan='2'>[[1jzk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Anadara_inaequivalvis Anadara inaequivalvis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JZK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JZK FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=1jzk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jzk OCA], [https://pdbe.org/1jzk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jzk RCSB], [https://www.ebi.ac.uk/pdbsum/1jzk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jzk 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=1jzk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jzk OCA], [https://pdbe.org/1jzk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jzk RCSB], [https://www.ebi.ac.uk/pdbsum/1jzk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jzk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/GLB1_ANAIN GLB1_ANAIN] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Anadara inaequivalvis]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Cushing | [[Category: Cushing L]] | ||
[[Category: Gibson | [[Category: Gibson QH]] | ||
[[Category: Knapp | [[Category: Knapp JE]] | ||
[[Category: Royer | [[Category: Royer Jr WE]] | ||
Latest revision as of 11:48, 16 August 2023
Crystal Structure of Scapharca inaequivalvis HbI, I114F mutant (deoxy)Crystal Structure of Scapharca inaequivalvis HbI, I114F mutant (deoxy)
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCooperative ligand binding in the dimeric hemoglobin from the blood clam Scapharca inaequivalvis results primarily from tertiary, rather than quaternary, structural changes. Ligand binding is coupled with conformational changes of key residues, including Phe 97, which is extruded from the proximal heme pocket, and the heme group, which moves deeper into the heme pocket. We have tested the role of the heme movement in cooperative function by mutating Ile 114, at the base of the heme pocket. Replacement of this residue with a Met did not disturb the hemoglobin structure or significantly alter equilibrium ligand binding properties. In contrast, substitution with a Phe at position 114 inhibits the ligand-linked movement of the heme group, and substantially reduces oxygen affinity and cooperativity. As the extent of heme movement to the normal position of the ligated state is diminished, Phe 97 is inhibited from its movement into the interface upon ligand binding. These results indicate a tight coupling between these two key cooperative transitions and suggest that the heme movement may be an obligatory trigger for expulsion of Phe 97 from the heme pocket. Restricting the ligand-linked heme movement in Scapharca dimeric hemoglobin reveals tight coupling between distal and proximal contributions to cooperativity.,Knapp JE, Gibson QH, Cushing L, Royer WE Jr Biochemistry. 2001 Dec 11;40(49):14795-805. PMID:11732898[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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