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4qys
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==TrpB2 enzymes== |
| + | <StructureSection load='4qys' size='340' side='right' caption='[[4qys]], [[Resolution|resolution]] 1.94Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4qys]] is a 2 chain structure. 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> | ||
| + | </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> | ||
| + | <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> | ||
| + | <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://www.rcsb.org/pdb/explore.do?structureId=4qys RCSB], [http://www.ebi.ac.uk/pdbsum/4qys PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[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. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | [[Category: | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Tryptophan synthase]] | ||
[[Category: Busch, F]] | [[Category: Busch, F]] | ||
[[Category: Loeffler, P]] | [[Category: Loeffler, P]] | ||
| + | [[Category: Merkl, R]] | ||
[[Category: Rajendran, C]] | [[Category: Rajendran, C]] | ||
| - | [[Category: | + | [[Category: Sterner, R]] |
| + | [[Category: Enzyme evolution]] | ||
| + | [[Category: Functional annotation]] | ||
| + | [[Category: Lyase]] | ||
Revision as of 13:01, 18 February 2015
TrpB2 enzymes
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