1kah: Difference between revisions

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-{{Seed}}
-[[Image:1kah.png|left|200px]]
-<!--
+==L-HISTIDINOL DEHYDROGENASE (HISD) STRUCTURE COMPLEXED WITH L-HISTIDINE (PRODUCT), ZN AND NAD (COFACTOR)==
-The line below this paragraph, containing "STRUCTURE_1kah", creates the "Structure Box" on the page.
+<StructureSection load='1kah' size='340' side='right'caption='[[1kah]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1kah]] 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=1KAH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KAH FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HIS:HISTIDINE'>HIS</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-{{STRUCTURE_1kah|  PDB=1kah  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kah OCA], [https://pdbe.org/1kah PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kah RCSB], [https://www.ebi.ac.uk/pdbsum/1kah PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kah ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ka/1kah_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1kah ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-===L-HISTIDINOL DEHYDROGENASE (HISD) STRUCTURE COMPLEXED WITH L-HISTIDINE (PRODUCT), ZN AND NAD (COFACTOR)===
+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:11842181<ref>PMID:11842181</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_11842181}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1kah" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 11842181 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_11842181}}
+__TOC__
+</StructureSection>
-==About this Structure==
-KAH 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=1KAH OCA].
-==Reference==
-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]
 [[Category: Escherichia coli]]
-[[Category: Histidinol dehydrogenase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Barbosa JARG]]
-[[Category: Barbosa, J A.R G.]]
+[[Category: Cygler M]]
-[[Category: Cygler, M.]]
+[[Category: Larocque R]]
-[[Category: Larocque, R.]]
+[[Category: Li Y]]
-[[Category: Li, Y.]]
+[[Category: Matte A]]
-[[Category: Matte, A.]]
+[[Category: Schrag JD]]
-[[Category: Schrag, J D.]]
+[[Category: Sivaraman J]]
-[[Category: Sivaraman, J.]]
-[[Category: 4 domain]]
-[[Category: Hisd]]
-[[Category: Homodimer]]
-[[Category: L-histidine biosynthesis]]
-[[Category: L-histidinol dehydrogenase]]
-[[Category: Nad cofactor]]
-[[Category: Rossman fold]]
-[[Category: Zinc]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 10:02:09 2008''