2jb4: Difference between revisions

Revision as of 09:35, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2jb4.png

Template:STRUCTURE 2jb4

ISOPENICILLIN N SYNTHASE WITH A 2-THIABICYCLOHEPTAN-6-ONE PRODUCT ANALOGUEISOPENICILLIN N SYNTHASE WITH A 2-THIABICYCLOHEPTAN-6-ONE PRODUCT ANALOGUE

Template:ABSTRACT PUBMED 17907118

About this StructureAbout this Structure

2JB4 is a Single protein structure of sequence from Emericella nidulans. Full crystallographic information is available from OCA.

ReferenceReference

A cyclobutanone analogue mimics penicillin in binding to isopenicillin N synthase., Stewart AC, Clifton IJ, Adlington RM, Baldwin JE, Rutledge PJ, Chembiochem. 2007 Nov 5;8(16):2003-7. PMID:17907118

The reaction cycle of isopenicillin N synthase observed by X-ray diffraction., Burzlaff NI, Rutledge PJ, Clifton IJ, Hensgens CM, Pickford M, Adlington RM, Roach PL, Baldwin JE, Nature. 1999 Oct 14;401(6754):721-4. PMID:10537113

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OCA

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 {{STRUCTURE_2jb4|  PDB=2jb4  |  SCENE=  }}
-'''ISOPENICILLIN N SYNTHASE WITH A 2-THIABICYCLOHEPTAN-6-ONE PRODUCT ANALOGUE'''
+===ISOPENICILLIN N SYNTHASE WITH A 2-THIABICYCLOHEPTAN-6-ONE PRODUCT ANALOGUE===
-==Overview==
+<!--
-A carbocyclic analogue of the beta-lactam antibiotic isopenicillin N (IPN) has been synthesised and cocrystallised with isopenicillin N synthase (IPNS), the central enzyme in the biosynthesis of penicillin antibiotics. The crystal structure of the IPNS-cyclobutanone complex reveals an active site environment similar to that seen in the enzyme-product complex generated by turnover of the natural substrate within the crystalline protein. The IPNS-cyclobutanone structure demonstrates that the product analogue is tethered to the protein by hydrogen bonding and salt bridge interactions with its carboxylate groups, as seen previously for the natural substrate and product. Furthermore, the successful cocrystallisation of this analogue with IPNS provides firm structural evidence for the utility of such cyclobutanone derivatives as hydrolytically stable analogues of bicyclic beta-lactams.
+The line below this paragraph, {{ABSTRACT_PUBMED_17907118}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17907118 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_17907118}}
 ==About this Structure==
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 ==Reference==
 A cyclobutanone analogue mimics penicillin in binding to isopenicillin N synthase., Stewart AC, Clifton IJ, Adlington RM, Baldwin JE, Rutledge PJ, Chembiochem. 2007 Nov 5;8(16):2003-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17907118 17907118]
+The reaction cycle of isopenicillin N synthase observed by X-ray diffraction., Burzlaff NI, Rutledge PJ, Clifton IJ, Hensgens CM, Pickford M, Adlington RM, Roach PL, Baldwin JE, Nature. 1999 Oct 14;401(6754):721-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10537113 10537113]
 [[Category: Emericella nidulans]]
 [[Category: Isopenicillin-N synthase]]
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 [[Category: Penicillin biosynthesis]]
 [[Category: Vitamin c]]
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