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1k75

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[[Image:1k75.jpg|left|200px]]
 
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==The L-histidinol dehydrogenase (hisD) structure implicates domain swapping and gene duplication.==
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The line below this paragraph, containing "STRUCTURE_1k75", creates the "Structure Box" on the page.
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<StructureSection load='1k75' size='340' side='right'caption='[[1k75]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1k75]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K75 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.75&#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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_1k75| PDB=1k75 | SCENE= }}
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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=1k75 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k75 OCA], [https://pdbe.org/1k75 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k75 RCSB], [https://www.ebi.ac.uk/pdbsum/1k75 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k75 ProSAT], [https://www.topsan.org/Proteins/BSGI/1k75 TOPSAN]</span></td></tr>
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</table>
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'''The L-histidinol dehydrogenase (hisD) structure implicates domain swapping and gene duplication.'''
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== Function ==
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[https://www.uniprot.org/uniprot/HISX_ECOLI HISX_ECOLI] Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.[HAMAP-Rule:MF_01024]
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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The histidine biosynthetic pathway is an ancient one found in bacteria, archaebacteria, fungi, and plants that converts 5-phosphoribosyl 1-pyrophosphate to l-histidine in 10 enzymatic reactions. This pathway provided a paradigm for the operon, transcriptional regulation of gene expression, and feedback inhibition of a pathway. l-histidinol dehydrogenase (HisD, EC ) catalyzes the last two steps in the biosynthesis of l-histidine: sequential NAD-dependent oxidations of l-histidinol to l-histidinaldehyde and then to l-histidine. HisD functions as a homodimer and requires the presence of one Zn(2+) cation per monomer. We have determined the three-dimensional structure of Escherichia coli HisD in the apo state as well as complexes with substrate, Zn(2+), and NAD(+) (best resolution is 1.7 A). Each monomer is made of four domains, whereas the intertwined dimer possibly results from domain swapping. Two domains display a very similar incomplete Rossmann fold that suggests an ancient event of gene duplication. Residues from both monomers form the active site. Zn(2+) plays a crucial role in substrate binding but is not directly involved in catalysis. The active site residue His-327 participates in acid-base catalysis, whereas Glu-326 activates a water molecule. NAD(+) binds weakly to one of the Rossmann fold domains in a manner different from that previously observed for other proteins having a Rossmann fold.
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Check<jmol>
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<jmolCheckbox>
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==About this Structure==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k7/1k75_consurf.spt"</scriptWhenChecked>
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1K75 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K75 OCA].
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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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==Reference==
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</jmolCheckbox>
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Mechanism of action and NAD+-binding mode revealed by the crystal structure of L-histidinol dehydrogenase., Barbosa JA, Sivaraman J, Li Y, Larocque R, Matte A, Schrag JD, Cygler M, Proc Natl Acad Sci U S A. 2002 Feb 19;99(4):1859-64. Epub 2002 Feb 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11842181 11842181]
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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=1k75 ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Histidinol dehydrogenase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Barbosa JARG]]
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[[Category: BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative.]]
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[[Category: Cygler M]]
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[[Category: Barbosa, J A.R G.]]
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[[Category: Larocque R]]
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[[Category: Cygler, M.]]
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[[Category: Li Y]]
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[[Category: Larocque, R.]]
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[[Category: Matte A]]
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[[Category: Li, Y.]]
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[[Category: Schrag J]]
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[[Category: Matte, A.]]
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[[Category: Sivaraman J]]
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[[Category: Schrag, J.]]
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[[Category: Sivaraman, J.]]
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[[Category: 4 domain]]
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[[Category: Bsgi]]
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[[Category: Hisd]]
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[[Category: Homodimer]]
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[[Category: L-histidine biosynthesis]]
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[[Category: L-histidinol dehydrogenase]]
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[[Category: Montreal-kingston bacterial structural genomics initiative]]
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[[Category: Nad cofactor]]
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[[Category: Rossman fold]]
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[[Category: Structural genomic]]
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[[Category: Zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:23:20 2008''
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Current revision

The L-histidinol dehydrogenase (hisD) structure implicates domain swapping and gene duplication.

PDB ID 1k75

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