1dvr: Difference between revisions
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==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== | ||
<StructureSection load='1dvr' size='340' side='right' caption='[[1dvr]], [[Resolution|resolution]] 2.36Å' scene=''> | <StructureSection load='1dvr' size='340' side='right'caption='[[1dvr]], [[Resolution|resolution]] 2.36Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1dvr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DVR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DVR FirstGlance]. <br> | <table><tr><td colspan='2'>[[1dvr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DVR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DVR FirstGlance]. <br> | ||
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==See Also== | ==See Also== | ||
*[[Adenylate kinase|Adenylate kinase]] | *[[Adenylate kinase 3D structures|Adenylate kinase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Adenylate kinase]] | [[Category: Adenylate kinase]] | ||
[[Category: Atcc 18824]] | [[Category: Atcc 18824]] | ||
[[Category: Large Structures]] | |||
[[Category: Schlauderer, G J]] | [[Category: Schlauderer, G J]] | ||
[[Category: Schulz, G E]] | [[Category: Schulz, G E]] | ||
[[Category: Myokinase]] | [[Category: Myokinase]] | ||
[[Category: Nucleoside monophosphate kinase]] | [[Category: Nucleoside monophosphate kinase]] | ||
Revision as of 13:11, 8 January 2020
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
Structural highlights
Function[KAD2_YEAST] Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways.[HAMAP-Rule:MF_03168][1] [2] [3] 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 PubMedStructural 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. 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[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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