1h72: Difference between revisions

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-[[Image:1h72.gif|left|200px]]<br />
-<applet load="1h72" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1h72, resolution 1.8&Aring;" />
-'''CRYSTAL STRUCTURE OF HOMOSERINE KINASE COMPLEXED WITH HSE'''<br />
-==Overview==
+==CRYSTAL STRUCTURE OF HOMOSERINE KINASE COMPLEXED WITH HSE==
-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 ... [[http://ispc.weizmann.ac.il/pmbin/getpm?11535056 (full description)]]
+<StructureSection load='1h72' size='340' side='right'caption='[[1h72]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+== Structural highlights ==
+<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>
+</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>
+<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.
-==About this Structure==
+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>
-H72 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Methanococcus_jannaschii Methanococcus jannaschii]] with HSE, ANP and TRS as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.39 2.7.1.39]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H72 OCA]].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11535056 11535056]
+</div>
-[[Category: Methanococcus jannaschii]]
+<div class="pdbe-citations 1h72" style="background-color:#fffaf0;"></div>
-[[Category: Single protein]]
+== References ==
-[[Category: Daugherty, M.]]
+<references/>
-[[Category: Krishna, S.S.]]
+__TOC__
-[[Category: Osterman, A.L.]]
+</StructureSection>
-[[Category: Zhang, H.]]
+[[Category: Large Structures]]
-[[Category: Zhou, T.]]
+[[Category: Methanocaldococcus jannaschii]]
-[[Category: ANP]]
+[[Category: Daugherty M]]
-[[Category: HSE]]
+[[Category: Krishna SS]]
-[[Category: TRS]]
+[[Category: Osterman AL]]
-[[Category: kinase]]
+[[Category: Zhang H]]
-[[Category: threonine biosynthesis]]
+[[Category: Zhou T]]
-[[Category: transferase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 16:11:56 2007''