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4r0m
From Proteopedia
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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=4r0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r0m OCA], [http://pdbe.org/4r0m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r0m RCSB], [http://www.ebi.ac.uk/pdbsum/4r0m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r0m ProSAT]</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=4r0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r0m OCA], [http://pdbe.org/4r0m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r0m RCSB], [http://www.ebi.ac.uk/pdbsum/4r0m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r0m ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Microcystins, which are the most common cause of hepatotoxicity associated with cyanobacterial water blooms, are assembled in vivo on a large multienzyme complex via a mixed nonribosomal peptide synthetase/polyketide synthetase (NRPS/PKS). The biosynthesis of microcystin in Microcystis aeruginosa PCC 7806 starts with the enzyme McyG, which contains an adenylation-peptidyl carrier protein (A-PCP) didomain for loading the starter unit to assemble the side chain of an Adda residue. However, the catalytic mechanism remains unclear. Here, the 2.45 A resolution crystal structure of the McyG A-PCP didomain complexed with the catalytic intermediate L-phenylalanyl-adenylate (L-Phe-AMP) is reported. Each asymmetric unit contains two protein molecules, one of which consists of the A-PCP didomain and the other of which comprises only the A domain. Structural analyses suggest that Val227 is likely to be critical for the selection of hydrophobic substrates. Moreover, two distinct interfaces demonstrating variable crosstalk between the PCP domain and the A domain were observed. A catalytic cycle for the adenylation and peptide transfer of the A-PCP didomain is proposed. | ||
| + | |||
| + | Structure of the adenylation-peptidyl carrier protein didomain of the Microcystis aeruginosa microcystin synthetase McyG.,Tan XF, Dai YN, Zhou K, Jiang YL, Ren YM, Chen Y, Zhou CZ Acta Crystallogr D Biol Crystallogr. 2015 Apr;71(Pt 4):873-81. doi:, 10.1107/S1399004715001716. Epub 2015 Mar 27. PMID:25849398<ref>PMID:25849398</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4r0m" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 08:23, 18 December 2019
Structure of McyG A-PCP complexed with phenylalanyl-adenylate
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Categories: Large Structures | Microcystis aeruginosa pcc 7806 | Chen, Y X | Dai, Y N | Jiang, Y L | Ren, Y M | Tan, X F | Zhou, C Z | Zhou, K | Acetyl-coa synthetase-like domain | Acyl carrier protein-like domain | Adenylation domain | Ligase | Peptidyl carrier protein like domain | Phenylalanyl-amp | Phenylalanyl-amp binding
