1ebf

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[[Image:1ebf.jpg|left|200px]]
 
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{{Structure
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==HOMOSERINE DEHYDROGENASE FROM S. CEREVISIAE COMPLEX WITH NAD+==
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|PDB= 1ebf |SIZE=350|CAPTION= <scene name='initialview01'>1ebf</scene>, resolution 2.30&Aring;
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<StructureSection load='1ebf' size='340' side='right'caption='[[1ebf]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>
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<table><tr><td colspan='2'>[[1ebf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EBF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EBF FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Homoserine_dehydrogenase Homoserine dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.3 1.1.1.3] </span>
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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]] 2.3&#8491;</td></tr>
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|GENE= HOM6P ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
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|DOMAIN=
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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=1ebf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ebf OCA], [https://pdbe.org/1ebf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ebf RCSB], [https://www.ebi.ac.uk/pdbsum/1ebf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ebf ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1ebu|1EBU]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ebf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ebf OCA], [http://www.ebi.ac.uk/pdbsum/1ebf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ebf RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/DHOM_YEAST DHOM_YEAST]
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== Evolutionary Conservation ==
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'''HOMOSERINE DEHYDROGENASE FROM S. CEREVISIAE COMPLEX WITH NAD+'''
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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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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eb/1ebf_consurf.spt"</scriptWhenChecked>
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The structure of the antifungal drug target homoserine dehydrogenase (HSD) was determined from Saccharomyces cerevisiae in apo and holo forms, and as a ternary complex with bound products, by X-ray diffraction. The three forms show that the enzyme is a dimer, with each monomer composed of three regions, the nucleotide-binding region, the dimerization region and the catalytic region. The dimerization and catalytic regions have novel folds, whereas the fold of the nucleotide-binding region is a variation on the Rossmann fold. The novel folds impose a novel composition and arrangement of active site residues when compared to all other currently known oxidoreductases. This observation, in conjunction with site-directed mutagenesis of active site residues and steady-state kinetic measurements, suggest that HSD exhibits a new variation on dehydrogenase chemistry.
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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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==About this Structure==
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</jmolCheckbox>
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1EBF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EBF OCA].
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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=1ebf ConSurf].
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<div style="clear:both"></div>
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==Reference==
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__TOC__
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Crystal structures of homoserine dehydrogenase suggest a novel catalytic mechanism for oxidoreductases., DeLaBarre B, Thompson PR, Wright GD, Berghuis AM, Nat Struct Biol. 2000 Mar;7(3):238-44. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10700284 10700284]
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</StructureSection>
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[[Category: Homoserine dehydrogenase]]
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Berghuis AM]]
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[[Category: Berghuis, A M.]]
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[[Category: DeLaBarre B]]
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[[Category: DeLaBarre, B.]]
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[[Category: Thompson PR]]
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[[Category: Thompson, P R.]]
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[[Category: Wright GD]]
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[[Category: Wright, G D.]]
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[[Category: dehydrogenase]]
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[[Category: dimer]]
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[[Category: dinucleotide]]
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[[Category: homoserine]]
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[[Category: nad]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:59:16 2008''
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Current revision

HOMOSERINE DEHYDROGENASE FROM S. CEREVISIAE COMPLEX WITH NAD+

PDB ID 1ebf

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