1dss

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[[Image:1dss.gif|left|200px]]
[[Image:1dss.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1dss |SIZE=350|CAPTION= <scene name='initialview01'>1dss</scene>, resolution 1.88&Aring;
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The line below this paragraph, containing "STRUCTURE_1dss", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AVG:Active+Site'>AVG</scene> and <scene name='pdbsite=AVR:Active+Site'>AVR</scene>
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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=CCS:CARBOXYMETHYLATED+CYSTEINE'>CCS</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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/Glyceraldehyde-3-phosphate_dehydrogenase_(phosphorylating) Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.12 1.2.1.12] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1dss| PDB=1dss | 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=1dss FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dss OCA], [http://www.ebi.ac.uk/pdbsum/1dss PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dss RCSB]</span>
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}}
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'''STRUCTURE OF ACTIVE-SITE CARBOXYMETHYLATED D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM PALINURUS VERSICOLOR'''
'''STRUCTURE OF ACTIVE-SITE CARBOXYMETHYLATED D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM PALINURUS VERSICOLOR'''
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==Reference==
==Reference==
Structure of active site carboxymethylated D-glyceraldehyde-3-phosphate dehydrogenase from Palinurus versicolor., Song SY, Xu YB, Lin ZJ, Tsou CL, J Mol Biol. 1999 Apr 9;287(4):719-25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10191140 10191140]
Structure of active site carboxymethylated D-glyceraldehyde-3-phosphate dehydrogenase from Palinurus versicolor., Song SY, Xu YB, Lin ZJ, Tsou CL, J Mol Biol. 1999 Apr 9;287(4):719-25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10191140 10191140]
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[[Category: Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)]]
 
[[Category: Palinurus versicolor]]
[[Category: Palinurus versicolor]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Lin, Z.]]
[[Category: Lin, Z.]]
[[Category: Song, S.]]
[[Category: Song, S.]]
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[[Category: the-half-of-sites reaction]]
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[[Category: The-half-of-sites reaction]]
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[[Category: active-site carboxymethylation]]
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[[Category: Active-site carboxymethylation]]
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[[Category: crystal structure]]
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[[Category: Crystal structure]]
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[[Category: d-glyceraldehyde-3-phosphate-dehydrogenase]]
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[[Category: D-glyceraldehyde-3-phosphate-dehydrogenase]]
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[[Category: molecular symmetry]]
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[[Category: Molecular symmetry]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:13:47 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:48:02 2008''
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Revision as of 11:13, 2 May 2008

Image:1dss.gif

Template:STRUCTURE 1dss

STRUCTURE OF ACTIVE-SITE CARBOXYMETHYLATED D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM PALINURUS VERSICOLOR


Overview

The structure of active site carboxymethylated D-glyceraldehyde-3-phosphate dehydrogenase from Palinurus versicolor was determined in the presence of coenzyme NAD+ at 1.88 A resolution with a final R-factor of 0.175. The structure refinement was carried out on the basis of the structure of holo-GAPDH at 2.0 A resolution using the program XPLOR. The carboxymethyl group connected to Cys149 is stabilized by a hydrogen bond between its OZ1 and Cys149N, and charge interaction between the carboxyl group and the nicotinamide moiety. The modification of Cys149 induced conformational changes in the active site, in particular, the site of sulphate ion 501 (the proposed attacking inorganic phosphate ion in catalysis), and segment 208-218 nearby. Extensive hydrogen-bonding interactions occur in the active site, which contribute to the higher stability of the modified enzyme. The modification of the active site did not affect the conformation of GAPDH elsewhere, including the subunit interfaces. The structures of the green and red subunits in the asymmetric unit are nearly identical, suggesting that the half-site reactivity of this enzyme is from ligand-induced rather than pre-existing asymmetry. It is proposed that the carboxymethyl group takes the place of the acyl group of the reaction intermediate, and the catalytic mechanism of this enzyme is discussed in the light of a comparison of the structures of the native and the carboxymethylated GAPDH.

About this Structure

1DSS is a Single protein structure of sequence from Palinurus versicolor. Full crystallographic information is available from OCA.

Reference

Structure of active site carboxymethylated D-glyceraldehyde-3-phosphate dehydrogenase from Palinurus versicolor., Song SY, Xu YB, Lin ZJ, Tsou CL, J Mol Biol. 1999 Apr 9;287(4):719-25. PMID:10191140 Page seeded by OCA on Fri May 2 14:13:47 2008

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