4sdh: Difference between revisions

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[[Image:4sdh.jpg|left|200px]]
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[[Image:4sdh.png|left|200px]]


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{{STRUCTURE_4sdh|  PDB=4sdh  |  SCENE=  }}  
{{STRUCTURE_4sdh|  PDB=4sdh  |  SCENE=  }}  


'''HIGH RESOLUTION CRYSTALLOGRAPHIC ANALYSIS OF A COOPERATIVE DIMERIC HEMOGLOBIN'''
===HIGH RESOLUTION CRYSTALLOGRAPHIC ANALYSIS OF A COOPERATIVE DIMERIC HEMOGLOBIN===




==Overview==
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High-resolution crystal structures of the co-operative dimeric hemoglobin from the blood clam Scapharca inaequivalvis have been determined in the unliganded (deoxy) and carbon monoxide (CO) liganded states. The deoxy structure has been refined at 1.6 A resolution to an R-factor of 0.158 and the CO structure has been refined at 1.4 A resolution to an R-factor of 0.159. These structures reveal details of the structural transitions involved in co-operative ligand binding that involve only a minor rotation of subunits but very striking tertiary changes at the interface. A small number of residues in the F-helix appear to mediate co-operativity in this simple hemoglobin. The oxygen affinity of each subunit appears to be largely dictated by the disposition of phenylalanine 97, whose side-chain packs in the heme pocket in the deoxy state but is extruded towards the interface in the CO-liganded structure. Direct involvement of the ligand-binding heme group is a novel feature of the subunit interface and appears important for intersubunit communication. Ligation alters the conformation of the heme propionate groups along with two interacting residues from the symmetry-related subunit. These two residues, lysine 96 and asparagine 100, link the heme of one subunit with the F-helix of the second subunit in such a way as to influence the ligand affinity of that subunit. The interface is highly hydrated by well-ordered water molecules that are likely to be important in the stabilization of the two structures.
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{{ABSTRACT_PUBMED_8289287}}


==About this Structure==
==About this Structure==
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[[Category: Royerjunior, W E.]]
[[Category: Royerjunior, W E.]]
[[Category: Oxygen transport]]
[[Category: Oxygen transport]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:29:22 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:50:20 2008''

Revision as of 10:50, 3 July 2008

File:4sdh.png

Template:STRUCTURE 4sdh

HIGH RESOLUTION CRYSTALLOGRAPHIC ANALYSIS OF A COOPERATIVE DIMERIC HEMOGLOBIN

Template:ABSTRACT PUBMED 8289287

About this Structure

4SDH is a Single protein structure of sequence from Scapharca inaequivalvis. This structure supersedes the now removed PDB entry 2sdh. Full crystallographic information is available from OCA.

Reference

High-resolution crystallographic analysis of a co-operative dimeric hemoglobin., Royer WE Jr, J Mol Biol. 1994 Jan 14;235(2):657-81. PMID:8289287

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