2fq1

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[[Image:2fq1.gif|left|200px]]<br /><applet load="2fq1" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2fq1.gif|left|200px]]
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caption="2fq1, resolution 2.30&Aring;" />
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'''Crystal structure of the two-domain non-ribosomal peptide synthetase EntB containing isochorismate lyase and aryl-carrier protein domains'''<br />
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{{Structure
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|PDB= 2fq1 |SIZE=350|CAPTION= <scene name='initialview01'>2fq1</scene>, resolution 2.30&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>
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|ACTIVITY= [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]
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|GENE= entB, entG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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}}
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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==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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2FQ1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FQ1 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16632253 16632253]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16632253 16632253]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Isochorismatase]]
[[Category: Isochorismatase]]
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[[Category: entb]]
[[Category: entb]]
[[Category: multi-domain]]
[[Category: multi-domain]]
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[[Category: nrps]]
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[[Category: nrp]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:23:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:55:28 2008''

Revision as of 14:55, 20 March 2008

Image:2fq1.gif


PDB ID 2fq1

Drag the structure with the mouse to rotate
, resolution 2.30Å
Ligands: , and
Gene: entB, entG (Escherichia coli)
Activity: Isochorismatase, with EC number 3.3.2.1
Coordinates: save as pdb, mmCIF, xml



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. 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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