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| - | [[Image:4cts.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_4cts| PDB=4cts | SCENE= }} | | {{STRUCTURE_4cts| PDB=4cts | SCENE= }} |
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| - | '''CRYSTAL STRUCTURE ANALYSIS AND MOLECULAR MODEL OF A COMPLEX OF CITRATE SYNTHASE WITH OXALOACETATE AND S-ACETONYL-COENZYME A'''
| + | ===CRYSTAL STRUCTURE ANALYSIS AND MOLECULAR MODEL OF A COMPLEX OF CITRATE SYNTHASE WITH OXALOACETATE AND S-ACETONYL-COENZYME A=== |
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| - | ==Overview==
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| - | The crystal structure of the complex of pig heart citrate synthase and oxaloacetate in the presence of the potent inhibitor S-acetonyl coenzyme A has been determined at a nominal resolution of 2.9 A by Patterson search techniques and refined by restrained crystallographic refinement. The complex crystallizes in the presence of polyvinylpyrrolidone in space group P4(3)2(1)2 with a = 101.5 A and c = 224.6 A, with one dimeric molecule of molecular weight 100,000 in the asymmetric unit. The crystallographic R factor is 0.194 for the 14,332 unique reflections between 6.0 and 2.9 A resolution. The structures of two forms of citrate synthase in the presence and absence of product molecules have been determined recently and shown to differ in the relative arrangement of the large and small domains ("closed" and "open" forms). The third crystal form described here is also closed, but there is substantial rearrangement within the small domain relative to either of the other crystal forms. We conclude that this is a third structural state of the enzyme, and catalytic activity of the enzyme depends on structural changes during the course of the reaction affecting domain conformation also. The three structures are compared, and it is shown that the large domain is considerably more rigid than the small domain. The conformation of the small domain adapts to the ligand. The inhibitor, and the "coenzyme-A-binding segment" of the enzyme are disordered. No electron density is observed for the inhibitor, and only weak density for the coenzyme-A-binding segment. Electron density for oxaloacetate is well defined. It binds in a very similar manner to citrate. | + | The line below this paragraph, {{ABSTRACT_PUBMED_6716477}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 6716477 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_6716477}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Wiegand, G.]] | | [[Category: Wiegand, G.]] |
| | [[Category: Oxo-acid-lyase]] | | [[Category: Oxo-acid-lyase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:22:49 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:33:57 2008'' |
Revision as of 10:33, 3 July 2008
Template:STRUCTURE 4cts
CRYSTAL STRUCTURE ANALYSIS AND MOLECULAR MODEL OF A COMPLEX OF CITRATE SYNTHASE WITH OXALOACETATE AND S-ACETONYL-COENZYME A
Template:ABSTRACT PUBMED 6716477
About this Structure
4CTS is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.
Reference
Crystal structure analysis and molecular model of a complex of citrate synthase with oxaloacetate and S-acetonyl-coenzyme A., Wiegand G, Remington S, Deisenhofer J, Huber R, J Mol Biol. 1984 Mar 25;174(1):205-19. PMID:6716477
Page seeded by OCA on Thu Jul 3 13:33:57 2008
