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1gpd

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[[Image:1gpd.gif|left|200px]]
[[Image:1gpd.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1gpd |SIZE=350|CAPTION= <scene name='initialview01'>1gpd</scene>, resolution 2.9&Aring;
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The line below this paragraph, containing "STRUCTURE_1gpd", 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=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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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|DOMAIN=
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{{STRUCTURE_1gpd| PDB=1gpd | 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=1gpd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gpd OCA], [http://www.ebi.ac.uk/pdbsum/1gpd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gpd RCSB]</span>
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}}
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'''STUDIES OF ASYMMETRY IN THE THREE-DIMENSIONAL STRUCTURE OF LOBSTER D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE'''
'''STUDIES OF ASYMMETRY IN THE THREE-DIMENSIONAL STRUCTURE OF LOBSTER D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE'''
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==Reference==
==Reference==
Studies of asymmetry in the three-dimensional structure of lobster D-glyceraldehyde-3-phosphate dehydrogenase., Moras D, Olsen KW, Sabesan MN, Buehner M, Ford GC, Rossmann MG, J Biol Chem. 1975 Dec 10;250(23):9137-62. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/127793 127793]
Studies of asymmetry in the three-dimensional structure of lobster D-glyceraldehyde-3-phosphate dehydrogenase., Moras D, Olsen KW, Sabesan MN, Buehner M, Ford GC, Rossmann MG, J Biol Chem. 1975 Dec 10;250(23):9137-62. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/127793 127793]
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[[Category: Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)]]
 
[[Category: Homarus americanus]]
[[Category: Homarus americanus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Rossmann, M G.]]
[[Category: Rossmann, M G.]]
[[Category: Sabesan, M N.]]
[[Category: Sabesan, M N.]]
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[[Category: oxido-reductse(aldehyde/donr,nad/accpt)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:51:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:48:40 2008''
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Revision as of 14:51, 2 May 2008

Template:STRUCTURE 1gpd

STUDIES OF ASYMMETRY IN THE THREE-DIMENSIONAL STRUCTURE OF LOBSTER D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE


Overview

An improved electron density map of lobster holo-D-glyceraldehyde-3-phosphate dehydrogenase has been computed to 2.9 A resolution based on two heavy atom isomorphous derivatives. This has been averaged only over the Q molecular 2-fold axis, which is known to be exact in the human holoenzyme. The map showed possible asymmetry between the subunits in which the active centers are closely related across the R axis (that is, between the red and green or between the yellow and blue subunits). A difference map between the electron density of citrate and sulfate-soaked crystals gave further evidence for possible asymmetry. The major differences of electron density between R axis-related subunits appear around the active center and suggest the following interpretations. 1. The conformation of the adenine about the glycosidic bond is the more frequently observed anti with a C-2' endo conformation for the ribose ring in the red and yellow subunits, but is probably syn with a C-3' endo conformation in the green and blue subunits.2. The adenine ribose has its 3'-hydroxyl group hydrogen-bonded to a main chain carbonyl group in the red and yellow subunits but not in the green and blue subunits, as a consequence of the differing ribose conformations. 3. Cysteine-149 is more closely associated with histidine-176 in the green and blue subunits, and appears nearer the nicotinamide in the red and yellow subunits.

About this Structure

1GPD is a Single protein structure of sequence from Homarus americanus. Full crystallographic information is available from OCA.

Reference

Studies of asymmetry in the three-dimensional structure of lobster D-glyceraldehyde-3-phosphate dehydrogenase., Moras D, Olsen KW, Sabesan MN, Buehner M, Ford GC, Rossmann MG, J Biol Chem. 1975 Dec 10;250(23):9137-62. PMID:127793 Page seeded by OCA on Fri May 2 17:51:17 2008

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