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1bjn

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(New page: 200px<br /> <applet load="1bjn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bjn, resolution 2.30&Aring;" /> '''STRUCTURE OF PHOSPH...)
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[[Image:1bjn.gif|left|200px]]<br />
 
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<applet load="1bjn" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1bjn, resolution 2.30&Aring;" />
 
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'''STRUCTURE OF PHOSPHOSERINE AMINOTRANSFERASE FROM ESCHERICHIA COLI'''<br />
 
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==Overview==
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==STRUCTURE OF PHOSPHOSERINE AMINOTRANSFERASE FROM ESCHERICHIA COLI==
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Phosphoserine aminotransferase (PSAT; EC 2.6.1.52), a member of subgroup, IV of the aminotransferases, catalyses the conversion of, 3-phosphohydroxypyruvate to l-phosphoserine. The crystal structure of PSAT, from Escherichia coli has been solved in space group P212121 using MIRAS, phases in combination with density modification and was refined to an, R-factor of 17.5% (Rfree=20.1 %) at 2.3 A resolution. In addition, the, structure of PSAT in complex with alpha-methyl-l-glutamate (AMG) has been, refined to an R-factor of 18.5% (Rfree=25.1%) at 2.8 A resolution. Each, subunit (361 residues) of the PSAT homodimer is composed of a large, pyridoxal-5'-phosphate binding domain (residues 16-268), consisting of a, seven-stranded mainly parallel beta-sheet, two additional beta-strands and, seven ... [[http://ispc.weizmann.ac.il/pmbin/getpm?10024454 (full description)]]
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<StructureSection load='1bjn' size='340' side='right'caption='[[1bjn]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1bjn]] is a 2 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=1BJN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BJN FirstGlance]. <br>
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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]] 2.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr>
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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=1bjn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bjn OCA], [https://pdbe.org/1bjn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bjn RCSB], [https://www.ebi.ac.uk/pdbsum/1bjn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bjn ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SERC_ECOLI SERC_ECOLI] Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine. Is involved in both pyridoxine and serine biosynthesis.<ref>PMID:2121717</ref> <ref>PMID:8706854</ref>
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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/bj/1bjn_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=1bjn ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1BJN is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.52 2.6.1.52]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BJN OCA]].
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*[[Phosphoserine aminotransferase|Phosphoserine aminotransferase]]
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== References ==
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==Reference==
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<references/>
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Crystal structure of phosphoserine aminotransferase from Escherichia coli at 2.3 A resolution: comparison of the unligated enzyme and a complex with alpha-methyl-l-glutamate., Hester G, Stark W, Moser M, Kallen J, Markovic-Housley Z, Jansonius JN, J Mol Biol. 1999 Feb 26;286(3):829-50. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10024454 10024454]
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Hester, G.]]
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[[Category: Hester G]]
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[[Category: Jansonius, J.N.]]
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[[Category: Jansonius JN]]
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[[Category: Moser, M.]]
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[[Category: Moser M]]
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[[Category: aminotransferase]]
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[[Category: l-serine biosynthesis]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 20:17:53 2007''
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Current revision

STRUCTURE OF PHOSPHOSERINE AMINOTRANSFERASE FROM ESCHERICHIA COLI

PDB ID 1bjn

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