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1fg3

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[[Image:1fg3.gif|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF L-HISTIDINOL PHOSPHATE AMINOTRANSFERASE COMPLEXED WITH L-HISTIDINOL==
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|PDB= 1fg3 |SIZE=350|CAPTION= <scene name='initialview01'>1fg3</scene>, resolution 2.2&Aring;
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<StructureSection load='1fg3' size='340' side='right'caption='[[1fg3]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene>
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<table><tr><td colspan='2'>[[1fg3]] is a 1 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=1FG3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FG3 FirstGlance]. <br>
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|ACTIVITY= [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]
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</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>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HSA:PHOSPHORIC+ACID+MONO-[2-AMINO-3-(3H-IMIDAZOL-4-YL)-PROPYL]ESTER'>HSA</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fg3 OCA], [https://pdbe.org/1fg3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fg3 RCSB], [https://www.ebi.ac.uk/pdbsum/1fg3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fg3 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HIS8_ECOLI HIS8_ECOLI]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fg/1fg3_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1fg3 ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE OF L-HISTIDINOL PHOSPHATE AMINOTRANSFERASE COMPLEXED WITH L-HISTIDINOL'''
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==See Also==
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*[[Aminotransferase 3D structures|Aminotransferase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The biosynthesis of histidine is a central metabolic process in organisms ranging from bacteria to yeast and plants. The seventh step in the synthesis of histidine within eubacteria is carried out by a pyridoxal-5'-phosphate (PLP)-dependent l-histidinol phosphate aminotransferase (HisC, EC 2.6.1.9). Here, we report the crystal structure of l-histidinol phosphate aminotransferase from Escherichia coli, as a complex with pyridoxamine-5'-phosphate (PMP) at 1.5 A resolution, as the internal aldimine with PLP, and in a covalent, tetrahedral complex consisting of PLP and l-histidinol phosphate attached to Lys214, both at 2.2 A resolution. This covalent complex resembles, in structural terms, the gem-diamine intermediate that is formed transiently during conversion of the internal to external aldimine.HisC is a dimeric enzyme with a mass of approximately 80 kDa. Like most PLP-dependent enzymes, each HisC monomer consists of two domains, a larger PLP-binding domain having an alpha/beta/alpha topology, and a smaller domain. An N-terminal arm contributes to the dimerization of the two monomers. The PLP-binding domain of HisC shows weak sequence similarity, but significant structural similarity with the PLP-binding domains of a number of PLP-dependent enzymes. Residues that interact with the PLP cofactor, including Tyr55, Asn157, Asp184, Tyr187, Ser213, Lys214 and Arg222, are conserved in the family of aspartate, tyrosine and histidinol phosphate aminotransferases. The imidazole ring of l-histidinol phosphate is bound, in part, through a hydrogen bond with Tyr110, a residue that is substituted by Phe in the broad substrate specific HisC enzymes from Zymomonas mobilis and Bacillus subtilis.Comparison of the structures of the HisC internal aldimine, the PMP complex and the HisC l-histidinol phosphate complex reveal minimal changes in protein or ligand structure. Proton transfer, required for conversion of the gem-diamine to the external aldimine, does not appear to be limited by the distance between substrate and lysine amino groups. We propose that the tetrahedral complex has resulted from non-productive binding of l-histidinol phosphate soaked into the HisC crystals, resulting in its inability to be converted to the external aldimine at the HisC active site.
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==About this Structure==
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1FG3 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=1FG3 OCA].
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==Reference==
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Crystal structure of histidinol phosphate aminotransferase (HisC) from Escherichia coli, and its covalent complex with pyridoxal-5'-phosphate and l-histidinol phosphate., Sivaraman J, Li Y, Larocque R, Schrag JD, Cygler M, Matte A, J Mol Biol. 2001 Aug 24;311(4):761-76. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11518529 11518529]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Histidinol-phosphate transaminase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Cygler M]]
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[[Category: Cygler, M.]]
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[[Category: Sivaraman J]]
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[[Category: Sivaraman, J.]]
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[[Category: PLP]]
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[[Category: aminotransferase]]
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[[Category: crystal structure]]
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[[Category: hisc]]
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[[Category: histidine biosynthesis]]
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[[Category: pyridoxal phosphate]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:08:37 2008''
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Current revision

CRYSTAL STRUCTURE OF L-HISTIDINOL PHOSPHATE AMINOTRANSFERASE COMPLEXED WITH L-HISTIDINOL

PDB ID 1fg3

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