1hdg

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(New page: 200px<br /><applet load="1hdg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hdg, resolution 2.5&Aring;" /> '''THE CRYSTAL STRUCTURE...)
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[[Image:1hdg.jpg|left|200px]]<br /><applet load="1hdg" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1hdg, resolution 2.5&Aring;" />
 
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'''THE CRYSTAL STRUCTURE OF HOLO-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM THE HYPERTHERMOPHILIC BACTERIUM THERMOTOGA MARITIMA AT 2.5 ANGSTROMS RESOLUTION'''<br />
 
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==Overview==
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==THE CRYSTAL STRUCTURE OF HOLO-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM THE HYPERTHERMOPHILIC BACTERIUM THERMOTOGA MARITIMA AT 2.5 ANGSTROMS RESOLUTION==
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The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase, from the hyperthermophile Thermotoga maritima was determined by Patterson, search methods using the known structure of the Bacillus, stearothermophilus enzyme. The structure was refined at a resolution of, 2.5 A to an R-factor of 16.63% for 26289 reflections between 8.0 A an 2.5, A with F &gt; 2 sigma(F). The crystallographic asymmetric unit contains two, monomers related by approximate 2-fold symmetry and a tetramer is built up, by crystallographic symmetry. The root-mean-square deviation of Ca, positions of glyceraldehyde-3-phosphate dehydrogenase from T. maritima and, B. stearothermophilus is 0.83 A in the NAD+ binding domains and smaller, close to the cofactor. In contrast, the largest deviations in the, catalytic domains are found at residues involved in coordination of, sulphate ion SO4 339, which most likely marks the site of the attacking, inorganic phosphate ion in catalysis. A large number of extra salt-bridges, may be an important factor contributing to the high thermostability of, this protein.
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<StructureSection load='1hdg' size='340' side='right'caption='[[1hdg]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1hdg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HDG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HDG FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hdg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hdg OCA], [https://pdbe.org/1hdg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hdg RCSB], [https://www.ebi.ac.uk/pdbsum/1hdg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hdg ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/G3P_THEMA G3P_THEMA]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hd/1hdg_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1hdg ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1HDG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with SO4 and NAD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HDG OCA].
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*[[Glyceraldehyde-3-phosphate dehydrogenase 3D structures|Glyceraldehyde-3-phosphate dehydrogenase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima at 2.5 A resolution., Korndorfer I, Steipe B, Huber R, Tomschy A, Jaenicke R, J Mol Biol. 1995 Mar 3;246(4):511-21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7877172 7877172]
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[[Category: Large Structures]]
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[[Category: Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)]]
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[[Category: Single protein]]
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[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
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[[Category: Huber, R.]]
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[[Category: Huber R]]
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[[Category: Jaenicke, R.]]
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[[Category: Jaenicke R]]
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[[Category: Korndoerfer, I.]]
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[[Category: Korndoerfer I]]
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[[Category: Steipe, B.]]
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[[Category: Steipe B]]
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[[Category: Tomschy, A.]]
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[[Category: Tomschy A]]
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[[Category: NAD]]
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[[Category: SO4]]
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[[Category: oxidoreductase (aldehy(d)-nad(a))]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:32:15 2007''
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Current revision

THE CRYSTAL STRUCTURE OF HOLO-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM THE HYPERTHERMOPHILIC BACTERIUM THERMOTOGA MARITIMA AT 2.5 ANGSTROMS RESOLUTION

PDB ID 1hdg

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