1dvr: Difference between revisions

Revision as of 23:41, 30 June 2008

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File:1dvr.png

Template:STRUCTURE 1dvr

STRUCTURE OF A MUTANT ADENYLATE KINASE LIGATED WITH AN ATP-ANALOGUE SHOWING DOMAIN CLOSURE OVER ATPSTRUCTURE OF A MUTANT ADENYLATE KINASE LIGATED WITH AN ATP-ANALOGUE SHOWING DOMAIN CLOSURE OVER ATP

Template:ABSTRACT PUBMED 8594191

About this StructureAbout this Structure

1DVR is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

Structure of a mutant adenylate kinase ligated with an ATP-analogue showing domain closure over ATP., Schlauderer GJ, Proba K, Schulz GE, J Mol Biol. 1996 Feb 23;256(2):223-7. PMID:8594191

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 {{STRUCTURE_1dvr|  PDB=1dvr  |  SCENE=  }}
-'''STRUCTURE OF A MUTANT ADENYLATE KINASE LIGATED WITH AN ATP-ANALOGUE SHOWING DOMAIN CLOSURE OVER ATP'''
+===STRUCTURE OF A MUTANT ADENYLATE KINASE LIGATED WITH AN ATP-ANALOGUE SHOWING DOMAIN CLOSURE OVER ATP===
-==Overview==
+<!--
-Structural studies on unligated and ligated adenylate kinases have shown that two domains, LID and NMPbind, close over the bound substrates, ATP and AMP, respectively. These motions can be, but need not be independent from each other. Up to now, the known structures display only the states "both domains open", "both closed" and "NMP bind closed". In spite of numerous cocrystallization attempts with ATP, a crystalline state "LID closed" has not yet been produced. These experiences suggested that LID closure depends on a bound AMP molecule, in contrast to enzyme kinetic studies indicating a random-bi-bi mechanism. Using an inactive mutant of yeast adenylate kinase together with the ATP analogue AMPPCF2P, however, we have now crystallized an adenylate kinase in the LID closed state. The structure was established at 2.36 A resolution; it indicates that the domain motions occur largely independent from each other in agreement with the kinetic studies. As a side-result, we report the protein environment of the fluorine atoms of the bound ATP analogue.
+The line below this paragraph, {{ABSTRACT_PUBMED_8594191}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8594191 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_8594191}}
 ==About this Structure==
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 [[Category: Myokinase]]
 [[Category: Nucleoside monophosphate kinase]]
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