3cq4: Difference between revisions

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-{{Seed}}
-[[Image:3cq4.png|left|200px]]
-<!--
+==Histidinol-phosphate aminotransferase from Corynebacterium glutamicum==
-The line below this paragraph, containing "STRUCTURE_3cq4", creates the "Structure Box" on the page.
+<StructureSection load='3cq4' size='340' side='right'caption='[[3cq4]], [[Resolution|resolution]] 2.20&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'>[[3cq4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_glutamicum Corynebacterium glutamicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CQ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CQ4 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]] 2.2&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
-{{STRUCTURE_3cq4|  PDB=3cq4  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3cq4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cq4 OCA], [https://pdbe.org/3cq4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cq4 RCSB], [https://www.ebi.ac.uk/pdbsum/3cq4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cq4 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/HIS8_CORGL HIS8_CORGL]
+== 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/cq/3cq4_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=3cq4 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Histidinol-phosphate aminotransferase (HisC) is a pyridoxal 5'-phosphate-dependent enzyme that catalyzes the reversible transamination reaction between histidinol phosphate (His-P) and 2-oxoglutarate (O-Glu). The crystal structures of apo histidinol-phosphate aminotransferase from Corynebacterium glutamicum, of the internal PLP aldimine adduct and of a pyridoxamine 5-phosphate-enzyme complex were determined at resolutions of 2.2, 2.1 and 1.8 A, respectively. Residues important for substrate specificity were identified by modelling His-P into the active site and comparison with crystal structures of HisC from Thermotoga maritima and Escherichia coli. Four of the residues lining the substrate-binding pocket were studied by site-directed mutagenesis. Kinetic analysis of the Tyr21Phe mutant suggested that the hydrogen bond between the side chain of this residue and the phosphate group of His-P is important for recognition of the natural substrate and discrimination against other potential amino donors such as phenylalanine and leucine. The mutagenesis studies further indicated that residue Asn99 does not contribute to the specific recognition of the amino-acid donor, but may be involved in binding of the phosphate group of pyridoxal 5'-phosphate. The conserved residues Tyr123 and Tyr257 interact with the substrate through van der Waals interactions and their potential for hydrogen-bonding interactions is not utilized in substrate recognition, as the corresponding phenylalanine mutants show only a moderate effect on the catalytic efficiency kcat/Km.
-===Histidinol-phosphate aminotransferase from Corynebacterium glutamicum===
+Insights into the structural basis of substrate recognition by histidinol-phosphate aminotransferase from Corynebacterium glutamicum.,Marienhagen J, Sandalova T, Sahm H, Eggeling L, Schneider G Acta Crystallogr D Biol Crystallogr. 2008 Jun;64(Pt 6):675-85. Epub 2008, May 14. PMID:18560156<ref>PMID:18560156</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3cq4" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_18560156}}, adds the Publication Abstract to the page
+*[[Aminotransferase 3D structures|Aminotransferase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 18560156 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_18560156}}
+__TOC__
+</StructureSection>
-==About this Structure==
-CQ4 is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Corynebacterium_glutamicum Corynebacterium glutamicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CQ4 OCA].
-==Reference==
-<ref group="xtra">PMID:18560156</ref><references group="xtra"/>
-[[Category: Corynebacterium glutamicum]]
-[[Category: Histidinol-phosphate transaminase]]
-[[Category: Marienhagen, J.]]
-[[Category: Sandalova, T.]]
-[[Category: Schneider, G.]]
-[[Category: Amino-acid biosynthesis]]
 [[Category: Corynebacterium glutamicum]]
-[[Category: Histidine biosynthesis]]
+[[Category: Large Structures]]
-[[Category: Histidinol-phosphate aminotransferase]]
+[[Category: Marienhagen J]]
-[[Category: Plp]]
+[[Category: Sandalova T]]
-[[Category: Pyridoxal phosphate]]
+[[Category: Schneider G]]
-[[Category: Strep-tag]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 06:58:59 2009''