View source for 3cq4


==Histidinol-phosphate aminotransferase from Corynebacterium glutamicum==
<StructureSection load='3cq4' size='340' side='right' caption='[[3cq4]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3cq4]] is a 2 chain structure with sequence 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CQ4 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3cq5|3cq5]], [[3cq6|3cq6]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HisC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1718 Corynebacterium glutamicum])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidinol-phosphate_transaminase Histidinol-phosphate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.9 2.6.1.9] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3cq4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cq4 OCA], [http://pdbe.org/3cq4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3cq4 RCSB], [http://www.ebi.ac.uk/pdbsum/3cq4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3cq4 ProSAT]</span></td></tr>
</table>
== 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].
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== 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.

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>
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<div class="pdbe-citations 3cq4" style="background-color:#fffaf0;"></div>

==See Also==
*[[Aminotransferase|Aminotransferase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Corynebacterium glutamicum]]
[[Category: Histidinol-phosphate transaminase]]
[[Category: Marienhagen, J]]
[[Category: Sandalova, T]]
[[Category: Schneider, G]]
[[Category: Amino-acid biosynthesis]]
[[Category: Histidine biosynthesis]]
[[Category: Histidinol-phosphate aminotransferase]]
[[Category: Plp]]
[[Category: Pyridoxal phosphate]]
[[Category: Strep-tag]]
[[Category: Transferase]]