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1hv4

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CRYSTAL STRUCTURE ANALYSIS OF BAR-HEAD GOOSE HEMOGLOBIN (DEOXY FORM)

Structural highlights

1hv4 is a 8 chain structure with sequence from Anser indicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.8Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HBA_ANSIN 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 a high oxygen affinity species of hemoglobin, bar-headed goose hemoglobin in deoxy form, has been determined to a resolution of 2.8 A. The R and R(free) factor of the model are 0.197 and 0.243, respectively. The structure reported here is a special deoxy state of hemoglobin and indicates the differences in allosteric mechanisms between the goose and human hemoglobins. The quaternary structure of the goose deoxy hemoglobin shows obvious differences from that of human deoxy hemoglobin. The rotation angle of one alphabeta dimer relative to its partner in a tetramer molecule from the goose oxy to deoxy hemoglobin is only 4.6 degrees, and the translation is only 0.3 A, which are much smaller than those in human hemoglobin. In the alpha(1)beta(2) switch region of the goose deoxy hemoglobin, the imidazole ring of His beta(2)97 does not span the side-chain of Thr alpha(1)41 relative to the oxy hemoglobin as in human hemoglobin. And the tertiary structure changes of heme pocket and FG corner are also smaller than that in human hemoglobin. A unique mutation among avian and mammalian Hbs of alpha119 from proline to alanine at the alpha(1)beta(1 )interface in bar-headed goose hemoglobin brings a gap between Ala alpha119 and Leu beta55, the minimum distance between the two residues is 4.66 A. At the entrance to the central cavity around the molecular dyad, some residues of two beta chains form a positively charged groove where the inositol pentaphosphate binds to the hemoglobin. The His beta146 is at the inositol pentaphosphate binding site and the salt-bridge between His beta146 and Asp beta94 does not exist in the deoxy hemoglobin, which brings the weak chloride-independent Bohr effect to bar-headed goose hemoglobin.

The crystal structure of bar-headed goose hemoglobin in deoxy form: the allosteric mechanism of a hemoglobin species with high oxygen affinity.,Liang Y, Hua Z, Liang X, Xu Q, Lu G J Mol Biol. 2001 Oct 12;313(1):123-37. PMID:11601851^[1]

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

References

↑ Liang Y, Hua Z, Liang X, Xu Q, Lu G. The crystal structure of bar-headed goose hemoglobin in deoxy form: the allosteric mechanism of a hemoglobin species with high oxygen affinity. J Mol Biol. 2001 Oct 12;313(1):123-37. PMID:11601851 doi:10.1006/jmbi.2001.5028

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/1hv4"

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1hv4]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Anser_indicus Anser indicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HV4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HV4 FirstGlance]. <br>
-</td></tr><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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#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;'>[[1a4f|1a4f]], [[1c40|1c40]]</div></td></tr>
+<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=1hv4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hv4 OCA], [https://pdbe.org/1hv4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hv4 RCSB], [https://www.ebi.ac.uk/pdbsum/1hv4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hv4 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/HBA_ANSIN HBA_ANSIN]] Involved in oxygen transport from the lung to the various peripheral tissues. [[https://www.uniprot.org/uniprot/HBB_ANSIN HBB_ANSIN]] Involved in oxygen transport from the lung to the various peripheral tissues.
+[https://www.uniprot.org/uniprot/HBA_ANSIN HBA_ANSIN] Involved in oxygen transport from the lung to the various peripheral tissues.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 38: / Line 38: @@
 [[Category: Anser indicus]]
 [[Category: Large Structures]]
-[[Category: Hua, Z]]
+[[Category: Hua Z]]
-[[Category: Liang, X]]
+[[Category: Liang X]]
-[[Category: Liang, Y]]
+[[Category: Liang Y]]
-[[Category: Lu, G]]
+[[Category: Lu G]]
-[[Category: Xu, Q]]
+[[Category: Xu Q]]
-[[Category: Allosteric mechanism]]
-[[Category: Heme]]
-[[Category: Oxygen storage-transport complex]]
-[[Category: Oxygen transport]]
-[[Category: Respiratory protein]]

1hv4

From Proteopedia

Current revision

CRYSTAL STRUCTURE ANALYSIS OF BAR-HEAD GOOSE HEMOGLOBIN (DEOXY FORM)

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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