4zm4
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | ''' | + | ==Complex structure of PctV K276R mutant with PMP and 3-dehydroshkimate== |
| + | <StructureSection load='4zm4' size='340' side='right' caption='[[4zm4]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4zm4]] is a 6 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZM4 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4zm3|4zm3]]</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=4zm4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zm4 OCA], [http://pdbe.org/4zm4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zm4 RCSB], [http://www.ebi.ac.uk/pdbsum/4zm4 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 4zm4" style="background-color:#fffaf0;"></div> | |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Eguchi, T]] | ||
| + | [[Category: Hirayama, A]] | ||
[[Category: Kudo, F]] | [[Category: Kudo, F]] | ||
| - | [[Category: Hirayama, A]] | ||
| - | [[Category: Eguchi, T]] | ||
[[Category: Miyanaga, A]] | [[Category: Miyanaga, A]] | ||
| + | [[Category: Aminotransferase]] | ||
| + | [[Category: Pyridoxal 5-phosphate]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 03:53, 16 October 2015
Complex structure of PctV K276R mutant with PMP and 3-dehydroshkimate
| |||||||||||
