1w3u

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{{Seed}}
 
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[[Image:1w3u.png|left|200px]]
 
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==Crystal structure of phosphoserine aminotransferase from Bacillus circulans var. alkalophilus==
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The line below this paragraph, containing "STRUCTURE_1w3u", creates the "Structure Box" on the page.
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<StructureSection load='1w3u' size='340' side='right'caption='[[1w3u]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1w3u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Niallia_circulans Niallia circulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W3U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W3U FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.5&#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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
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{{STRUCTURE_1w3u| PDB=1w3u | SCENE= }}
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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=1w3u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w3u OCA], [https://pdbe.org/1w3u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w3u RCSB], [https://www.ebi.ac.uk/pdbsum/1w3u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w3u ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SERC_NIACI SERC_NIACI] Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.<ref>PMID:16532449</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/w3/1w3u_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=1w3u ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The crystal structure of the vitamin B(6)-dependent enzyme phosphoserine aminotransferase from the obligatory alkaliphile Bacillus alcalophilus has been determined at 1.08 A resolution. The model was refined to an R-factor of 11.7% (R(free) = 13.9%). The enzyme displays a narrow pH optimum of enzymatic activity at pH 9.0. The final structure was compared to the previously reported structure of the mesophilic phosphoserine aminotransferase from Escherichia coli and to that of phosphoserine aminotransferase from a facultative alkaliphile, Bacillus circulans subsp. alkalophilus. All three enzymes are homodimers with each monomer comprising a two-domain architecture. Despite the high structural similarity, the alkaliphilic representatives possess a set of distinctive structural features. Two residues directly interacting with pyridoxal-5'-phosphate are replaced, and an additional hydrogen bond to the O3' atom of the cofactor is present in alkaliphilic phosphoserine aminotransferases. The number of hydrogen bonds and hydrophobic interactions at the dimer interface is increased. Hydrophobic interactions between the two domains in the monomers are enhanced. Moreover, the number of negatively charged amino acid residues increases on the solvent-accessible molecular surface and fewer hydrophobic residues are exposed to the solvent. Further, the total amount of ion pairs and ion networks is significantly reduced in the Bacillus enzymes, while the total number of hydrogen bonds is increased. The mesophilic enzyme from Escherichia coli contains two additional beta-strands in a surface loop with a third beta-strand being shorter in the structure. The identified structural features are proposed to be possible factors implicated in the alkaline adaptation of phosphoserine aminotransferase.
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===CRYSTAL STRUCTURE OF PHOSPHOSERINE AMINOTRANSFERASE FROM BACILLUS CIRCULANS VAR. ALKALOPHILUS===
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Enzyme adaptation to alkaline pH: atomic resolution (1.08 A) structure of phosphoserine aminotransferase from Bacillus alcalophilus.,Dubnovitsky AP, Kapetaniou EG, Papageorgiou AC Protein Sci. 2005 Jan;14(1):97-110. PMID:15608117<ref>PMID:15608117</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1w3u" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_15608117}}, adds the Publication Abstract to the page
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*[[Phosphoserine aminotransferase|Phosphoserine aminotransferase]]
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(as it appears on PubMed at http://www.pubmed.gov), where 15608117 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15608117}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1W3U is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_circulans Bacillus circulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W3U OCA].
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[[Category: Niallia circulans]]
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[[Category: Dubnovitsky AP]]
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==Reference==
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[[Category: Kapetaniou EG]]
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Enzyme adaptation to alkaline pH: atomic resolution (1.08 A) structure of phosphoserine aminotransferase from Bacillus alcalophilus., Dubnovitsky AP, Kapetaniou EG, Papageorgiou AC, Protein Sci. 2005 Jan;14(1):97-110. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15608117 15608117]
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[[Category: Papageorgiou AC]]
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[[Category: Bacillus circulans]]
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[[Category: Phosphoserine transaminase]]
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[[Category: Single protein]]
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[[Category: Dubnovitsky, A P.]]
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[[Category: Kapetaniou, E G.]]
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[[Category: Papageorgiou, A C.]]
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[[Category: Phosphoserine aminotransferase]]
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[[Category: Pyridine serine biosynthesis]]
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[[Category: Pyridoxal-5'-phosphate transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:45:02 2008''
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Current revision

Crystal structure of phosphoserine aminotransferase from Bacillus circulans var. alkalophilus

PDB ID 1w3u

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