2fq1: Difference between revisions

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[[Image:2fq1.~~gif~~|left|200px]]

[[Image:2fq1.png|left|200px]]

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

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

~~==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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_16632253}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 16632253 is the PubMed ID number.

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==About this Structure==

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[[Category: Multi-domain]]

[[Category: Nrp]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 04~~:11:24 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:31:37 2008''

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-[[Image:2fq1.gif|left|200px]]
+{{Seed}}
+[[Image:2fq1.png|left|200px]]
 <!--
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 {{STRUCTURE_2fq1|  PDB=2fq1  |  SCENE=  }}
-'''Crystal structure of the two-domain non-ribosomal peptide synthetase EntB containing isochorismate lyase and aryl-carrier protein domains'''
+===Crystal structure of the two-domain non-ribosomal peptide synthetase EntB containing isochorismate lyase and aryl-carrier protein domains===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16632253}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16632253 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16632253}}
 ==About this Structure==
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 [[Category: Multi-domain]]
 [[Category: Nrp]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 04:11:24 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:31:37 2008''