2duu: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2duu]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Synechococcus_elongatus_pcc_7942 Synechococcus elongatus pcc 7942]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DUU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DUU FirstGlance]. <br> | <table><tr><td colspan='2'>[[2duu]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Synechococcus_elongatus_pcc_7942 Synechococcus elongatus pcc 7942]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DUU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DUU FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2d2i|2d2i]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2d2i|2d2i]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glyceraldehyde-3-phosphate_dehydrogenase_(NADP(+))_(phosphorylating) Glyceraldehyde-3-phosphate dehydrogenase (NADP(+)) (phosphorylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.13 1.2.1.13] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glyceraldehyde-3-phosphate_dehydrogenase_(NADP(+))_(phosphorylating) Glyceraldehyde-3-phosphate dehydrogenase (NADP(+)) (phosphorylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.13 1.2.1.13] </span></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2duu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2duu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2duu RCSB], [http://www.ebi.ac.uk/pdbsum/2duu PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2duu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2duu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2duu RCSB], [http://www.ebi.ac.uk/pdbsum/2duu PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Synechococcus elongatus pcc 7942]] | [[Category: Synechococcus elongatus pcc 7942]] | ||
[[Category: Kinoshita, T | [[Category: Kinoshita, T]] | ||
[[Category: Kitatani, T | [[Category: Kitatani, T]] | ||
[[Category: Nakamura, Y | [[Category: Nakamura, Y]] | ||
[[Category: Shigeoka, S | [[Category: Shigeoka, S]] | ||
[[Category: Tada, T | [[Category: Tada, T]] | ||
[[Category: Tamoi, M | [[Category: Tamoi, M]] | ||
[[Category: Wada, K | [[Category: Wada, K]] | ||
[[Category: Apo-form]] | [[Category: Apo-form]] | ||
[[Category: Glyceraldehyde 3-phosphate dehydrogenase]] | [[Category: Glyceraldehyde 3-phosphate dehydrogenase]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: Rossmann fold]] | [[Category: Rossmann fold]] | ||
Revision as of 21:43, 15 January 2015
Crystal Structure of apo-form of NADP-Dependent Glyceraldehyde-3-Phosphate Dehydrogenase from Synechococcus Sp.Crystal Structure of apo-form of NADP-Dependent Glyceraldehyde-3-Phosphate Dehydrogenase from Synechococcus Sp.
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of NADP-dependent apo-glyceraldehyde-3-phosphate dehydrogenase (apo-GAPDH) from Synechococcus PCC 7942 is reported. The crystal structure was solved by molecular replacement and refined to an R of 21.7% and R(free) of 27.5% at 2.9 angstroms resolution. The structural features of apo-GAPDH are as follows. The S-loop has an extremely flexible conformation and the sulfate ion is only taken into the classical P(i) site. A structural comparison with holo-GAPDHs indicated that the S-loop fixation is essential in the discrimination of NADP and NAD molecules. Structure of apo-glyceraldehyde-3-phosphate dehydrogenase from Synechococcus PCC7942.,Kitatani T, Nakamura Y, Wada K, Kinoshita T, Tamoi M, Shigeoka S, Tada T Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Aug 1;62(Pt, 8):727-30. Epub 2006 Jul 29. PMID:16880542[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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