4qys: Difference between revisions

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'''Unreleased structure'''
==TrpB2 enzymes==
<StructureSection load='4qys' size='340' side='right' caption='[[4qys]], [[Resolution|resolution]] 1.94&Aring;' 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.


The entry 4qys is ON HOLD  until Paper Publication
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>


Authors: Busch, F., Rajendran, C., Loeffler, P., Merkl, R., Sterner, R.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
Description: TrpB2 enzymes
== References ==
[[Category: Unreleased Structures]]
<references/>
[[Category: Sterner, R]]
__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: Merkl, R]]
[[Category: Sterner, R]]
[[Category: Enzyme evolution]]
[[Category: Functional annotation]]
[[Category: Lyase]]
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