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| - | [[Image:1gpd.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1gpd| PDB=1gpd | SCENE= }} | | {{STRUCTURE_1gpd| PDB=1gpd | SCENE= }} |
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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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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_127793}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 127793 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_127793}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Rossmann, M G.]] | | [[Category: Rossmann, M G.]] |
| | [[Category: Sabesan, M N.]] | | [[Category: Sabesan, M N.]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:51:17 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:38:39 2008'' |
Revision as of 02:38, 1 July 2008
Template:STRUCTURE 1gpd
STUDIES OF ASYMMETRY IN THE THREE-DIMENSIONAL STRUCTURE OF LOBSTER D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE
Template:ABSTRACT PUBMED 127793
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 Tue Jul 1 05:38:39 2008
