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3k9w

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Revision as of 06:14, 1 November 2017

Crystal structure of phosphopantetheine adenylyltransferase from Burkholderia pseudomallei with hydrolyzed 3'-dephospho Coenzyme A

Structural highlights

3k9w is a 1 chain structure with sequence from Burp1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , ,
Related:	3ikz
Gene:	coaD, BURPS1710b_0748 (BURP1)
Activity:	Pantetheine-phosphate adenylyltransferase, with EC number 2.7.7.3
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[COAD_BURP1] Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Phosphopantetheine adenylyltransferase (PPAT) catalyzes the fourth of five steps in the coenzyme A biosynthetic pathway, reversibly transferring an adenylyl group from ATP onto 4'-phosphopantetheine to yield dephospho-coenzyme A and pyrophosphate. Burkholderia pseudomallei is a soil- and water-borne pathogenic bacterium and the etiologic agent of melioidosis, a potentially fatal systemic disease present in southeast Asia. Two crystal structures are presented of the PPAT from B. pseudomallei with the expectation that, because of the importance of the enzyme in coenzyme A biosynthesis, they will aid in the search for defenses against this pathogen. A crystal grown in ammonium sulfate yielded a 2.1 A resolution structure that contained dephospho-coenzyme A with partial occupancy. The overall structure and ligand-binding interactions are quite similar to other bacterial PPAT crystal structures. A crystal grown at low pH in the presence of coenzyme A yielded a 1.6 A resolution structure in the same crystal form. However, the experimental electron density was not reflective of fully ordered coenzyme A, but rather was only reflective of an ordered 4'-diphosphopantetheine moiety.

Structures of phosphopantetheine adenylyltransferase from Burkholderia pseudomallei.,Edwards TE, Leibly DJ, Bhandari J, Statnekov JB, Phan I, Dieterich SH, Abendroth J, Staker BL, Van Voorhis WC, Myler PJ, Stewart LJ Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Sep 1;67(Pt, 9):1032-7. Epub 2011 Aug 13. PMID:21904046^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Edwards TE, Leibly DJ, Bhandari J, Statnekov JB, Phan I, Dieterich SH, Abendroth J, Staker BL, Van Voorhis WC, Myler PJ, Stewart LJ. Structures of phosphopantetheine adenylyltransferase from Burkholderia pseudomallei. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Sep 1;67(Pt, 9):1032-7. Epub 2011 Aug 13. PMID:21904046 doi:10.1107/S1744309111004349

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3k9w"

@@ Line 1: / Line 1: @@
 ==Crystal structure of phosphopantetheine adenylyltransferase from Burkholderia pseudomallei with hydrolyzed 3'-dephospho Coenzyme A==
 <StructureSection load='3k9w' size='340' side='right' caption='[[3k9w]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">coaD, BURPS1710b_0748 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=320372 BURP1])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pantetheine-phosphate_adenylyltransferase Pantetheine-phosphate adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.3 2.7.7.3] </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=3k9w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k9w OCA], [http://pdbe.org/3k9w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3k9w RCSB], [http://www.ebi.ac.uk/pdbsum/3k9w PDBsum]</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=3k9w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k9w OCA], [http://pdbe.org/3k9w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3k9w RCSB], [http://www.ebi.ac.uk/pdbsum/3k9w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3k9w ProSAT]</span></td></tr>
 </table>
 == Function ==

3k9w

From Proteopedia

Revision as of 06:14, 1 November 2017

Crystal structure of phosphopantetheine adenylyltransferase from Burkholderia pseudomallei with hydrolyzed 3'-dephospho Coenzyme A

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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