1qr0

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[[Image:1qr0.jpg|left|200px]]
[[Image:1qr0.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1qr0 |SIZE=350|CAPTION= <scene name='initialview01'>1qr0</scene>, resolution 1.90&Aring;
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The line below this paragraph, containing "STRUCTURE_1qr0", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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or leave the SCENE parameter empty for the default display.
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|GENE= SFP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])
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-->
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|DOMAIN=
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{{STRUCTURE_1qr0| PDB=1qr0 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qr0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qr0 OCA], [http://www.ebi.ac.uk/pdbsum/1qr0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qr0 RCSB]</span>
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}}
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'''CRYSTAL STRUCTURE OF THE 4'-PHOSPHOPANTETHEINYL TRANSFERASE SFP-COENZYME A COMPLEX'''
'''CRYSTAL STRUCTURE OF THE 4'-PHOSPHOPANTETHEINYL TRANSFERASE SFP-COENZYME A COMPLEX'''
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[[Category: Mofid, R M.]]
[[Category: Mofid, R M.]]
[[Category: Reuter, K.]]
[[Category: Reuter, K.]]
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[[Category: protein-coenzyme a complex]]
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[[Category: Protein-coenzyme a complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:36:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:17:44 2008''
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Revision as of 03:36, 3 May 2008

Image:1qr0.jpg

Template:STRUCTURE 1qr0

CRYSTAL STRUCTURE OF THE 4'-PHOSPHOPANTETHEINYL TRANSFERASE SFP-COENZYME A COMPLEX


Overview

The Bacillus subtilis Sfp protein activates the peptidyl carrier protein (PCP) domains of surfactin synthetase by transferring the 4'-phosphopantetheinyl moiety of coenzyme A (CoA) to a serine residue conserved in all PCPs. Its wide PCP substrate spectrum renders Sfp a biotechnologically valuable enzyme for use in combinatorial non-ribosomal peptide synthesis. The structure of the Sfp-CoA complex determined at 1.8 A resolution reveals a novel alpha/beta-fold exhibiting an unexpected intramolecular 2-fold pseudosymmetry. This suggests a similar fold and dimerization mode for the homodimeric phosphopantetheinyl transferases such as acyl carrier protein synthase. The active site of Sfp accommodates a magnesium ion, which is complexed by the CoA pyrophosphate, the side chains of three acidic amino acids and one water molecule. CoA is bound in a fashion that differs in many aspects from all known CoA-protein complex structures. The structure reveals regions likely to be involved in the interaction with the PCP substrate.

About this Structure

1QR0 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

Crystal structure of the surfactin synthetase-activating enzyme sfp: a prototype of the 4'-phosphopantetheinyl transferase superfamily., Reuter K, Mofid MR, Marahiel MA, Ficner R, EMBO J. 1999 Dec 1;18(23):6823-31. PMID:10581256 Page seeded by OCA on Sat May 3 06:36:16 2008

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