View source for 4zm4


==Complex structure of PctV K276R mutant with PMP and 3-dehydroshkimate==
<StructureSection load='4zm4' size='340' side='right'caption='[[4zm4]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4zm4]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_pactum Streptomyces pactum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZM4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZM4 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=P3B:(3E,4R,5R)-4,5-DIHYDROXY-3-{[(Z)-{3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4(1H)-YLIDENE}METHYL]IMINO}CYCLOHEX-1-ENE-1-CARBOXYLIC+ACID'>P3B</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4zm4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zm4 OCA], [https://pdbe.org/4zm4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zm4 RCSB], [https://www.ebi.ac.uk/pdbsum/4zm4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zm4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A8R0K5_9ACTN A8R0K5_9ACTN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mutational analysis of the pyridoxal 5'-phosphate (PLP)-dependent enzyme PctV has been carried out to elucidate the multi-step reaction mechanism for the formation of 3-aminobenzoate (3-ABA) from 3-dehydroshikimate (3-DSA). The results revealed that the introduction of a K276R mutation led to the accumulation of a quinonoid intermediate with an absorption maximum of 580 nm following the reaction of pyridoxamine 5'-phosphate (PMP) with 3-DSA. Furthermore, the chemical structure of this intermediate was supported by X-ray crystallographic analysis of the complex formed between the K276R mutant and the quinonoid intermediate. These results clearly show that a quinonoid intermediate is involved in the formation of 3-ABA, and also indicate that the Lys276 residue in the active site of the PctV enzyme plays multiple roles including acid/base catalysis during the dehydration reaction of the quinonoid intermediate, as well as assisting in the PMP formation and aminotransfer reaction.

Mechanism-based Trapping of the Quinonoid Intermediate Using the K276R Mutant of PLP-Dependent 3-Aminobenzoate Synthase PctV in the Biosynthesis of Pactamycin.,Hirayama A, Miyanaga A, Kudo F, Eguchi T Chembiochem. 2015 Oct 1. doi: 10.1002/cbic.201500426. PMID:26426567<ref>PMID:26426567</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4zm4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces pactum]]
[[Category: Eguchi T]]
[[Category: Hirayama A]]
[[Category: Kudo F]]
[[Category: Miyanaga A]]