1dvr

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[[Image:1dvr.jpg|left|200px]]
[[Image:1dvr.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1dvr |SIZE=350|CAPTION= <scene name='initialview01'>1dvr</scene>, resolution 2.36&Aring;
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The line below this paragraph, containing "STRUCTURE_1dvr", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=ATF:PHOSPHODIFLUOROMETHYLPHOSPHONIC+ACID-ADENYLATE+ESTER'>ATF</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenylate_kinase Adenylate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.3 2.7.4.3] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1dvr| PDB=1dvr | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dvr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dvr OCA], [http://www.ebi.ac.uk/pdbsum/1dvr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dvr RCSB]</span>
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}}
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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'''
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[[Category: Schlauderer, G J.]]
[[Category: Schlauderer, G J.]]
[[Category: Schulz, G E.]]
[[Category: Schulz, G E.]]
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[[Category: myokinase]]
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[[Category: Myokinase]]
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[[Category: nucleoside monophosphate kinase]]
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[[Category: Nucleoside monophosphate kinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:20:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:49:44 2008''
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Revision as of 11:20, 2 May 2008

Template:STRUCTURE 1dvr

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.

About this Structure

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

Reference

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 Page seeded by OCA on Fri May 2 14:20:24 2008

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