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2zlv

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Revision as of 07:38, 10 February 2016

Horse methemoglobin high salt, pH 7.0 (79% relative humidity)

Structural highlights

2zlv is a 2 chain structure with sequence from Equus caballus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1y8k, 1y8i, 1y8h, 1lfq, 1jy7, 1lfl, 2zlt, 2zlu, 2zlw, 2zlx
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[HBA_HORSE] Involved in oxygen transport from the lung to the various peripheral tissues. [HBB_HORSE] Involved in oxygen transport from the lung to the various peripheral tissues.

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 crystal structure of high-salt horse methaemoglobin has been determined at environmental relative humidities (r.h.) of 88, 79, 75 and 66%. The molecule is in the R state in the native and the r.h. 88% crystals. At r.h. 79%, the water content of the crystal is reduced and the molecule appears to move towards the R2 state. The crystals undergo a water-mediated transformation involving a doubling of one of the unit-cell parameters and an increase in water content when the environmental humidity is further reduced to r.h. 75%. The water content is now similar to that in the native crystals and the molecules are in the R state. The crystal structure at r.h. 66% is similar, but not identical, to that at r.h. 75%, but the solvent content is substantially reduced and the molecules have a quaternary structure that is in between those corresponding to the R and R2 states. Thus, variation in hydration leads to variation in the quaternary structure. Furthermore, partial dehydration appears to shift the structure from the R state to the R2 state. This observation is in agreement with the earlier conclusion that the changes in protein structure that accompany partial dehydration are similar to those that occur during protein action.

Water-mediated variability in the structure of relaxed-state haemoglobin.,Kaushal PS, Sankaranarayanan R, Vijayan M Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Jun 1;64(Pt, 6):463-9. Epub 2008 May 17. PMID:18540052^[1]

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

References

↑ Kaushal PS, Sankaranarayanan R, Vijayan M. Water-mediated variability in the structure of relaxed-state haemoglobin. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Jun 1;64(Pt, 6):463-9. Epub 2008 May 17. PMID:18540052 doi:http://dx.doi.org/10.1107/S1744309108013109

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/2zlv"

@@ Line 5: / Line 5: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1y8k|1y8k]], [[1y8i|1y8i]], [[1y8h|1y8h]], [[1lfq|1lfq]], [[1jy7|1jy7]], [[1lfl|1lfl]], [[2zlt|2zlt]], [[2zlu|2zlu]], [[2zlw|2zlw]], [[2zlx|2zlx]]</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=2zlv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zlv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zlv RCSB], [http://www.ebi.ac.uk/pdbsum/2zlv PDBsum]</span></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=2zlv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zlv OCA], [http://pdbe.org/2zlv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zlv RCSB], [http://www.ebi.ac.uk/pdbsum/2zlv PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 17: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2zlv ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 27: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2zlv" style="background-color:#fffaf0;"></div>
 ==See Also==

2zlv

From Proteopedia

Revision as of 07:38, 10 February 2016

Horse methemoglobin high salt, pH 7.0 (79% relative humidity)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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