6iow
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 6iow is ON HOLD Authors: Kezuka, Y., Yoshida, Y., Nonaka, T. Description: Crystal structure of Porphyromonas gingivalis phosphotransacetylase [[Cat...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Porphyromonas gingivalis phosphotransacetylase== | |
| + | <StructureSection load='6iow' size='340' side='right'caption='[[6iow]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6iow]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Porphyromonas_gingivalis_ATCC_33277 Porphyromonas gingivalis ATCC 33277]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IOW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IOW 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]] 1.7Å</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=6iow FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iow OCA], [https://pdbe.org/6iow PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6iow RCSB], [https://www.ebi.ac.uk/pdbsum/6iow PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6iow ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/B2RK03_PORG3 B2RK03_PORG3] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Acetyl phosphate (AcP) is generally produced from acetyl coenzyme A by phosphotransacetylase (Pta), and subsequent reaction with ADP, catalyzed by acetate kinase (Ack), produces ATP. The mechanism of ATP production in Porphyromonas gingivalis is poorly understood. The aim of this study was to explore the molecular basis of the Pta-Ack pathway in this microorganism. Pta and Ack from P. gingivalis ATCC 33277 were enzymatically and structurally characterized. Structural and mutational analyses suggest that Pta is a dimer with two substrate-binding sites in each subunit. Ack is also dimeric, with a catalytic cleft in each subunit, and structural analysis indicates a dramatic domain motion that opens and closes the cleft during catalysis. ATP formation by Ack proceeds via a sequential mechanism. Reverse transcription-PCR analysis demonstrated that the pta (PGN_1179) and ack (PGN_1178) genes, tandemly located in the genome, are cotranscribed as an operon. Inactivation of pta or ack in P. gingivalis by homologous recombination was successful only when the inactivated gene was expressed in trans. Therefore, both pta and ack genes are essential for this microorganism. Insights into the Pta-Ack pathway reported herein would be helpful to understand the energy acquisition in P. gingivalis. | ||
| - | + | Characterization of the phosphotransacetylase-acetate kinase pathway for ATP production in Porphyromonas gingivalis.,Yoshida Y, Sato M, Nonaka T, Hasegawa Y, Kezuka Y J Oral Microbiol. 2019 Apr 4;11(1):1588086. doi: 10.1080/20002297.2019.1588086., eCollection 2019. PMID:31007866<ref>PMID:31007866</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 6iow" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: Nonaka | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Porphyromonas gingivalis ATCC 33277]] | ||
| + | [[Category: Kezuka Y]] | ||
| + | [[Category: Nonaka T]] | ||
| + | [[Category: Yoshida Y]] | ||
Current revision
Crystal structure of Porphyromonas gingivalis phosphotransacetylase
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