4qys

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<StructureSection load='4qys' size='340' side='right'caption='[[4qys]], [[Resolution|resolution]] 1.94&Aring;' scene=''>
<StructureSection load='4qys' size='340' side='right'caption='[[4qys]], [[Resolution|resolution]] 1.94&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4qys]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Sacs2 Sacs2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QYS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QYS FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4qys]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus_P2 Saccharolobus solfataricus P2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QYS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QYS FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PLR:(5-HYDROXY-4,6-DIMETHYLPYRIDIN-3-YL)METHYL+DIHYDROGEN+PHOSPHATE'>PLR</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
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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]] 1.939&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">trpB2, SSO1145 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273057 SACS2])</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=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PLR:(5-HYDROXY-4,6-DIMETHYLPYRIDIN-3-YL)METHYL+DIHYDROGEN+PHOSPHATE'>PLR</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tryptophan_synthase Tryptophan synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.20 4.2.1.20] </span></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=4qys FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qys OCA], [https://pdbe.org/4qys PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qys RCSB], [https://www.ebi.ac.uk/pdbsum/4qys PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qys ProSAT]</span></td></tr>
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<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=4qys FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qys OCA], [http://pdbe.org/4qys PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qys RCSB], [http://www.ebi.ac.uk/pdbsum/4qys PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qys ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/TRPB2_SULSO TRPB2_SULSO]] The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
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[https://www.uniprot.org/uniprot/TRPB2_SACS2 TRPB2_SACS2] The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The rapid increase of the number of sequenced genomes asks for the functional annotation of the encoded enzymes. We used a combined computational-structural approach to determine the function of the TrpB2 subgroup of the tryptophan synthase beta chain/beta chain-like TrpB1-TrpB2 family (IPR023026). The results showed that TrpB2 enzymes are O-phospho-l-serine dependent tryptophan synthases, whereas TrpB1 enzymes catalyze the l-serine dependent synthesis of tryptophan. We found a single residue being responsible for the different substrate specificities of TrpB1 and TrpB2 and confirmed this finding by mutagenesis studies and crystallographic analysis of a TrpB2 enzyme with bound O-phospho-l-serine.
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TrpB2 enzymes are O-phospho-l-serine dependent tryptophan synthases.,Busch F, Rajendran C, Mayans O, Loffler P, Merkl R, Sterner R Biochemistry. 2014 Sep 30;53(38):6078-83. doi: 10.1021/bi500977y. Epub 2014 Sep, 17. PMID:25184516<ref>PMID:25184516</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 4qys" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[Tryptophan synthase|Tryptophan synthase]]
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*[[Tryptophan synthase 3D structures|Tryptophan synthase 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Sacs2]]
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[[Category: Saccharolobus solfataricus P2]]
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[[Category: Tryptophan synthase]]
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[[Category: Busch F]]
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[[Category: Busch, F]]
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[[Category: Loeffler P]]
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[[Category: Loeffler, P]]
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[[Category: Merkl R]]
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[[Category: Merkl, R]]
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[[Category: Rajendran C]]
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[[Category: Rajendran, C]]
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[[Category: Sterner R]]
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[[Category: Sterner, R]]
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[[Category: Enzyme evolution]]
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[[Category: Functional annotation]]
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[[Category: Lyase]]
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Current revision

TrpB2 enzymes

PDB ID 4qys

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