1gdh: Difference between revisions

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-[[Image:1gdh.gif|left|200px]]
- {{Structure
+==CRYSTAL STRUCTURE OF A NAD-DEPENDENT D-GLYCERATE DEHYDROGENASE AT 2.4 ANGSTROMS RESOLUTION==
-|PDB= 1gdh |SIZE=350|CAPTION= <scene name='initialview01'>1gdh</scene>, resolution 2.4&Aring;
+<StructureSection load='1gdh' size='340' side='right'caption='[[1gdh]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
+<table><tr><td colspan='2'>[[1gdh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Hyphomicrobium_methylovorum Hyphomicrobium methylovorum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GDH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GDH FirstGlance]. <br>
-|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycerate_dehydrogenase Glycerate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.29 1.1.1.29] </span>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-|DOMAIN=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gdh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gdh OCA], [https://pdbe.org/1gdh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gdh RCSB], [https://www.ebi.ac.uk/pdbsum/1gdh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gdh ProSAT]</span></td></tr>
-|RELATEDENTRY=
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gdh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gdh OCA], [http://www.ebi.ac.uk/pdbsum/1gdh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gdh RCSB]</span>
+== Function ==
-}}
+[https://www.uniprot.org/uniprot/DHGY_HYPME DHGY_HYPME] Active on hydroxypyruvate and glyoxylate.
+== Evolutionary Conservation ==
-'''CRYSTAL STRUCTURE OF A NAD-DEPENDENT D-GLYCERATE DEHYDROGENASE AT 2.4 ANGSTROMS RESOLUTION'''
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
-==Overview==
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gd/1gdh_consurf.spt"</scriptWhenChecked>
-D-Glycerate dehydrogenase (GDH) catalyzes the NADH-linked reduction of hydroxypyruvate to D-glycerate. GDH is a member of a family of NAD-dependent dehydrogenases that is characterized by a specificity for the D-isomer of the hydroxyacid substrate. The crystal structure of the apoenzyme form of GDH from Hyphomicrobium methylovorum has been determined by the method of isomorphous replacement and refined at 2.4 A resolution using a restrained least-squares method. The crystallographic R-factor is 19.4% for all 24,553 measured reflections between 10.0 and 2.4 A resolution. The GDH molecule is a symmetrical dimer composed of subunits of molecular mass 38,000, and shares significant structural homology with another NAD-dependent enzyme, formate dehydrogenase. The GDH subunit consists of two structurally similar domains that are approximately related to each other by 2-fold symmetry. The domains are separated by a deep cleft that forms the putative NAD and substrate binding sites. One of the domains has been identified as the NAD-binding domain based on its close structural similarity to the NAD-binding domains of other NAD-dependent dehydrogenases. The topology of the second domain is different from that found in the various catalytic domains of other dehydrogenases. A model of a ternary complex of GDH has been built in which putative catalytic residues are identified based on sequence homology between the D-isomer specific dehydrogenases. A structural comparison between GDH and L-lactate dehydrogenase indicates a convergence of active site residues and geometries for these two enzymes. The reactions catalyzed are chemically equivalent but of opposing stereospecificity. A hypothesis is presented to explain how the two enzymes may exploit the same coenzyme stereochemistry and a similar spatial arrangement of catalytic residues to carry out reactions that proceed to opposite enantiomers.
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
-==About this Structure==
+  </jmolCheckbox>
-GDH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Hyphomicrobium_methylovorum Hyphomicrobium methylovorum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GDH OCA].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1gdh ConSurf].
+<div style="clear:both"></div>
-==Reference==
+__TOC__
-Crystal structure of a NAD-dependent D-glycerate dehydrogenase at 2.4 A resolution., Goldberg JD, Yoshida T, Brick P, J Mol Biol. 1994 Mar 4;236(4):1123-40. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8120891 8120891]
+</StructureSection>
-[[Category: Glycerate dehydrogenase]]
 [[Category: Hyphomicrobium methylovorum]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Brick, P.]]
+[[Category: Brick P]]
-[[Category: Goldberg, J D.]]
+[[Category: Goldberg JD]]
-[[Category: Yoshida, T.]]
+[[Category: Yoshida T]]
-[[Category: oxidoreductase(choh (d)-nad(p)+ (a))]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:41:53 2008''