2fq1

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{{STRUCTURE_2fq1| PDB=2fq1 | SCENE= }}
{{STRUCTURE_2fq1| PDB=2fq1 | SCENE= }}
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'''Crystal structure of the two-domain non-ribosomal peptide synthetase EntB containing isochorismate lyase and aryl-carrier protein domains'''
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===Crystal structure of the two-domain non-ribosomal peptide synthetase EntB containing isochorismate lyase and aryl-carrier protein domains===
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==Overview==
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Nonribosomal peptide synthetases are modular proteins that operate in an assembly line fashion to bind, modify, and link amino acids. In the E. coli enterobactin NRPS system, the EntE adenylation domain catalyzes the transfer of a molecule of 2,3-dihydroxybenzoic acid to the pantetheine cofactor of EntB. We present here the crystal structure of the EntB protein that contains an N-terminal isochorismate lyase domain that functions in the synthesis of 2,3-dihydroxybenzoate and a C-terminal carrier protein domain. Functional analysis showed that the EntB-EntE interaction was surprisingly tolerant of a number of point mutations on the surface of EntB and EntE. Mutational studies on EntE support our previous hypothesis that members of the adenylate-forming family of enzymes adopt two distinct conformations to catalyze the two-step reactions.
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{{ABSTRACT_PUBMED_16632253}}
==About this Structure==
==About this Structure==
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[[Category: Multi-domain]]
[[Category: Multi-domain]]
[[Category: Nrp]]
[[Category: Nrp]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:11:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:31:37 2008''

Revision as of 02:31, 29 July 2008

Image:2fq1.png

Template:STRUCTURE 2fq1

Crystal structure of the two-domain non-ribosomal peptide synthetase EntB containing isochorismate lyase and aryl-carrier protein domains

Template:ABSTRACT PUBMED 16632253

About this Structure

2FQ1 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structure of the EntB multidomain nonribosomal peptide synthetase and functional analysis of its interaction with the EntE adenylation domain., Drake EJ, Nicolai DA, Gulick AM, Chem Biol. 2006 Apr;13(4):409-19. PMID:16632253

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