From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:3sdh.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:3sdh.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_3sdh| PDB=3sdh | SCENE= }} | | {{STRUCTURE_3sdh| PDB=3sdh | SCENE= }} |
| | | | |
| - | '''HIGH RESOLUTION CRYSTALLOGRAPHIC ANALYSIS OF A COOPERATIVE DIMERIC HEMOGLOBIN'''
| + | ===HIGH RESOLUTION CRYSTALLOGRAPHIC ANALYSIS OF A COOPERATIVE DIMERIC HEMOGLOBIN=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_8289287}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8289287 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_8289287}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 24: |
Line 28: |
| | [[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 22:12:53 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:06:35 2008'' |
Revision as of 10:06, 3 July 2008
Template:STRUCTURE 3sdh
HIGH RESOLUTION CRYSTALLOGRAPHIC ANALYSIS OF A COOPERATIVE DIMERIC HEMOGLOBIN
Template:ABSTRACT PUBMED 8289287
About this Structure
3SDH is a Single protein structure of sequence from Scapharca inaequivalvis. This structure supersedes the now removed PDB entry 1sdh. 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
Page seeded by OCA on Thu Jul 3 13:06:35 2008
