3pgk: Difference between revisions

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New page: left|200px<br /> <applet load="3pgk" size="450" color="white" frame="true" align="right" spinBox="true" caption="3pgk, resolution 2.5Å" /> '''THE STRUCTURE OF YEA...
 
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[[Image:3pgk.gif|left|200px]]<br />
[[Image:3pgk.gif|left|200px]]<br /><applet load="3pgk" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="3pgk" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="3pgk, resolution 2.5&Aring;" />
caption="3pgk, resolution 2.5&Aring;" />
'''THE STRUCTURE OF YEAST PHOSPHOGLYCERATE KINASE AT 0.25 NM RESOLUTION'''<br />
'''THE STRUCTURE OF YEAST PHOSPHOGLYCERATE KINASE AT 0.25 NM RESOLUTION'''<br />


==Overview==
==Overview==
The structure of yeast phosphoglycerate kinase has been determined with, data obtained from amino acid sequence, nucleotide sequence, and X-ray, crystallographic studies. The substrate binding sites, as deduced from, electron density maps, are compatible with known substrate specificity and, the stereochemical requirements for the enzymic reaction. A, carboxyl-imidazole interaction appears to be involved in controlling the, transition between the open and closed forms of the enzyme.
The structure of yeast phosphoglycerate kinase has been determined with data obtained from amino acid sequence, nucleotide sequence, and X-ray crystallographic studies. The substrate binding sites, as deduced from electron density maps, are compatible with known substrate specificity and the stereochemical requirements for the enzymic reaction. A carboxyl-imidazole interaction appears to be involved in controlling the transition between the open and closed forms of the enzyme.


==About this Structure==
==About this Structure==
3PGK 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 MG, ACE, ATP and 3PG as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 1PGK. The following page contains interesting information on the relation of 3PGK with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb50_1.html The Glycolytic Enzymes]]. Active as [http://en.wikipedia.org/wiki/Phosphoglycerate_kinase Phosphoglycerate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.3 2.7.2.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=3PGK OCA].  
3PGK 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=MG:'>MG</scene>, <scene name='pdbligand=ACE:'>ACE</scene>, <scene name='pdbligand=ATP:'>ATP</scene> and <scene name='pdbligand=3PG:'>3PG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1PGK. The following page contains interesting information on the relation of 3PGK with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb50_1.html The Glycolytic Enzymes]]. Active as [http://en.wikipedia.org/wiki/Phosphoglycerate_kinase Phosphoglycerate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.3 2.7.2.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PGK OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: The Glycolytic Enzymes]]
[[Category: The Glycolytic Enzymes]]
[[Category: Shaw, P.J.]]
[[Category: Shaw, P J.]]
[[Category: Walker, N.P.]]
[[Category: Walker, N P.]]
[[Category: Watson, H.C.]]
[[Category: Watson, H C.]]
[[Category: 3PG]]
[[Category: 3PG]]
[[Category: ACE]]
[[Category: ACE]]
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[[Category: phosphotransferase(carboxyl as acceptor)]]
[[Category: phosphotransferase(carboxyl as acceptor)]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:10:32 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:10:50 2008''

Revision as of 20:10, 21 February 2008

File:3pgk.gif


3pgk, resolution 2.5Å

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THE STRUCTURE OF YEAST PHOSPHOGLYCERATE KINASE AT 0.25 NM RESOLUTION

OverviewOverview

The structure of yeast phosphoglycerate kinase has been determined with data obtained from amino acid sequence, nucleotide sequence, and X-ray crystallographic studies. The substrate binding sites, as deduced from electron density maps, are compatible with known substrate specificity and the stereochemical requirements for the enzymic reaction. A carboxyl-imidazole interaction appears to be involved in controlling the transition between the open and closed forms of the enzyme.

About this StructureAbout this Structure

3PGK is a Single protein structure of sequence from Saccharomyces cerevisiae with , , and as ligands. This structure supersedes the now removed PDB entry 1PGK. The following page contains interesting information on the relation of 3PGK with [The Glycolytic Enzymes]. Active as Phosphoglycerate kinase, with EC number 2.7.2.3 Full crystallographic information is available from OCA.

ReferenceReference

Sequence and structure of yeast phosphoglycerate kinase., Watson HC, Walker NP, Shaw PJ, Bryant TN, Wendell PL, Fothergill LA, Perkins RE, Conroy SC, Dobson MJ, Tuite MF, et al., EMBO J. 1982;1(12):1635-40. PMID:6765200

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