1uky: Difference between revisions

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New page: left|200px<br /><applet load="1uky" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uky, resolution 2.13Å" /> '''SUBSTRATE SPECIFICIT...
 
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[[Image:1uky.jpg|left|200px]]<br /><applet load="1uky" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1uky.jpg|left|200px]]<br /><applet load="1uky" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1uky, resolution 2.13&Aring;" />
caption="1uky, resolution 2.13&Aring;" />
'''SUBSTRATE SPECIFICITY AND ASSEMBLY OF CATALYTIC CENTER DERIVED FROM TWO STRUCTURES OF LIGATED URIDYLATE KINASE'''<br />
'''SUBSTRATE SPECIFICITY AND ASSEMBLY OF CATALYTIC CENTER DERIVED FROM TWO STRUCTURES OF LIGATED URIDYLATE KINASE'''<br />


==Overview==
==Overview==
Two crystal structures of ligated uridylate kinase from Saccharomyces, cerevisiae were determined by X-ray analyses. The ligands were ADP and, AMP. Cocrystallization with ATP yielded crystals with ADP at the ATP site, and a mixture of AMP and ADP at the NMP site. Cocrystallization with ADP, gave rise to a distinct crystal type with ADP at the ATP site, but only, AMP at the NMP site. In both cases, the substrates are kept in place by, favorable crystal contacts. The structures have been refined to R-factors, of 17.8% and 19.6% at resolutions of 2.1 A and 1.9 A, respectively. A, comparison with the related cytosolic adenylate kinase from pig disclosed, large induced-fit movements on substrate binding and the disassembly of, the catalytic center in the absence of substrates. The relatively high, side-activity of uridylate kinase for AMP is explained by the finding that, the binding pocket is sized for an AMP, but constructed to bind UMP, together with a water molecule.
Two crystal structures of ligated uridylate kinase from Saccharomyces cerevisiae were determined by X-ray analyses. The ligands were ADP and AMP. Cocrystallization with ATP yielded crystals with ADP at the ATP site and a mixture of AMP and ADP at the NMP site. Cocrystallization with ADP gave rise to a distinct crystal type with ADP at the ATP site, but only AMP at the NMP site. In both cases, the substrates are kept in place by favorable crystal contacts. The structures have been refined to R-factors of 17.8% and 19.6% at resolutions of 2.1 A and 1.9 A, respectively. A comparison with the related cytosolic adenylate kinase from pig disclosed large induced-fit movements on substrate binding and the disassembly of the catalytic center in the absence of substrates. The relatively high side-activity of uridylate kinase for AMP is explained by the finding that the binding pocket is sized for an AMP, but constructed to bind UMP together with a water molecule.


==About this Structure==
==About this Structure==
1UKY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with ADP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UKY OCA].  
1UKY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UKY OCA].  


==Reference==
==Reference==
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Mueller-Dieckmann, H.J.]]
[[Category: Mueller-Dieckmann, H J.]]
[[Category: Schulz, G.E.]]
[[Category: Schulz, G E.]]
[[Category: ADP]]
[[Category: ADP]]
[[Category: transferase]]
[[Category: transferase]]


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Revision as of 16:25, 21 February 2008

File:1uky.jpg


1uky, resolution 2.13Å

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SUBSTRATE SPECIFICITY AND ASSEMBLY OF CATALYTIC CENTER DERIVED FROM TWO STRUCTURES OF LIGATED URIDYLATE KINASE

OverviewOverview

Two crystal structures of ligated uridylate kinase from Saccharomyces cerevisiae were determined by X-ray analyses. The ligands were ADP and AMP. Cocrystallization with ATP yielded crystals with ADP at the ATP site and a mixture of AMP and ADP at the NMP site. Cocrystallization with ADP gave rise to a distinct crystal type with ADP at the ATP site, but only AMP at the NMP site. In both cases, the substrates are kept in place by favorable crystal contacts. The structures have been refined to R-factors of 17.8% and 19.6% at resolutions of 2.1 A and 1.9 A, respectively. A comparison with the related cytosolic adenylate kinase from pig disclosed large induced-fit movements on substrate binding and the disassembly of the catalytic center in the absence of substrates. The relatively high side-activity of uridylate kinase for AMP is explained by the finding that the binding pocket is sized for an AMP, but constructed to bind UMP together with a water molecule.

About this StructureAbout this Structure

1UKY is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Substrate specificity and assembly of the catalytic center derived from two structures of ligated uridylate kinase., Muller-Dieckmann HJ, Schulz GE, J Mol Biol. 1995 Mar 3;246(4):522-30. PMID:7877173

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