2fq1
From Proteopedia
(New page: 200px<br /><applet load="2fq1" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fq1, resolution 2.30Å" /> '''Crystal structure of...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:2fq1.gif|left|200px]]<br /><applet load="2fq1" size=" | + | [[Image:2fq1.gif|left|200px]]<br /><applet load="2fq1" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2fq1, resolution 2.30Å" /> | caption="2fq1, resolution 2.30Å" /> | ||
'''Crystal structure of the two-domain non-ribosomal peptide synthetase EntB containing isochorismate lyase and aryl-carrier protein domains'''<br /> | '''Crystal structure of the two-domain non-ribosomal peptide synthetase EntB containing isochorismate lyase and aryl-carrier protein domains'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Nonribosomal peptide synthetases are modular proteins that operate in an | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 2FQ1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MG, CL and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Isochorismatase Isochorismatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.1 3.3.2.1] Full crystallographic information is available from [http:// | + | 2FQ1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Isochorismatase Isochorismatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.1 3.3.2.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FQ1 OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Isochorismatase]] | [[Category: Isochorismatase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Drake, E | + | [[Category: Drake, E J.]] |
| - | [[Category: Gulick, A | + | [[Category: Gulick, A M.]] |
| - | [[Category: Nicolai, D | + | [[Category: Nicolai, D A.]] |
[[Category: CL]] | [[Category: CL]] | ||
[[Category: EDO]] | [[Category: EDO]] | ||
| Line 25: | Line 25: | ||
[[Category: nrps]] | [[Category: nrps]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:23:58 2008'' |
Revision as of 15:23, 21 February 2008
|
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.
About this Structure
2FQ1 is a Single protein structure of sequence from Escherichia coli with , and as ligands. Active as Isochorismatase, with EC number 3.3.2.1 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
Page seeded by OCA on Thu Feb 21 17:23:58 2008
Categories: Escherichia coli | Isochorismatase | Single protein | Drake, E J. | Gulick, A M. | Nicolai, D A. | CL | EDO | MG | Acp | Entb | Multi-domain | Nrps
