1h72: Difference between revisions

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-[[Image:1h72.png|left|200px]]
-<!--
+==CRYSTAL STRUCTURE OF HOMOSERINE KINASE COMPLEXED WITH HSE==
-The line below this paragraph, containing "STRUCTURE_1h72", creates the "Structure Box" on the page.
+<StructureSection load='1h72' size='340' side='right'caption='[[1h72]], [[Resolution|resolution]] 1.80&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'>[[1h72]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H72 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H72 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]] 1.8&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=HSE:L-HOMOSERINE'>HSE</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
-{{STRUCTURE_1h72|  PDB=1h72  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1h72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h72 OCA], [https://pdbe.org/1h72 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h72 RCSB], [https://www.ebi.ac.uk/pdbsum/1h72 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h72 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/KHSE_METJA KHSE_METJA] Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate (By similarity).
+== 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/h7/1h72_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=1h72 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Homoserine kinase (HSK), the fourth enzyme in the aspartate pathway of amino acid biosynthesis, catalyzes the phosphorylation of L-homoserine (Hse) to L-homoserine phosphate, an intermediate in the production of L-threonine, L-isoleucine, and in higher plants, L-methionine. The high-resolution structures of Methanococcus jannaschii HSK ternary complexes with its amino acid substrate and ATP analogues have been determined by X-ray crystallography. These structures reveal the structural determinants of the tight and highly specific binding of Hse, which is coupled with local conformational changes that enforce the sequestration of the substrate. The delta-hydroxyl group of bound Hse is only 3.4 A away from the gamma-phosphate of the bound nucleotide, poised for the in-line attack at the gamma-phosphorus. The bound nucleotides are flexible at the triphosphate tail. Nevertheless, a Mg(2+) was located in one of the complexes that binds between the beta- and gamma-phosphates of the nucleotide with good ligand geometry and is coordinated by the side chain of Glu130. No strong nucleophile (base) can be located near the phosphoryl acceptor hydroxyl group. Therefore, we propose that the catalytic mechanism of HSK does not involve a catalytic base for activating the phosphoryl acceptor hydroxyl but instead is mediated via a transition state stabilization mechanism.
-===CRYSTAL STRUCTURE OF HOMOSERINE KINASE COMPLEXED WITH HSE===
+Structural basis for the catalysis and substrate specificity of homoserine kinase.,Krishna SS, Zhou T, Daugherty M, Osterman A, Zhang H Biochemistry. 2001 Sep 11;40(36):10810-8. PMID:11535056<ref>PMID:11535056</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_11535056}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1h72" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 11535056 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_11535056}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-[[1h72]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H72 OCA].
-==Reference==
-<ref group="xtra">PMID:11535056</ref><ref group="xtra">PMID:11188689</ref><references group="xtra"/>
-[[Category: Homoserine kinase]]
 [[Category: Methanocaldococcus jannaschii]]
-[[Category: Daugherty, M.]]
+[[Category: Daugherty M]]
-[[Category: Krishna, S S.]]
+[[Category: Krishna SS]]
-[[Category: Osterman, A L.]]
+[[Category: Osterman AL]]
-[[Category: Zhang, H.]]
+[[Category: Zhang H]]
-[[Category: Zhou, T.]]
+[[Category: Zhou T]]
-[[Category: Kinase]]
-[[Category: Threonine biosynthesis]]
-[[Category: Transferase]]