1i7q

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[[Image:1i7q.jpg|left|200px]]<br /><applet load="1i7q" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1i7q.jpg|left|200px]]
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caption="1i7q, resolution 1.95&Aring;" />
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'''ANTHRANILATE SYNTHASE FROM S. MARCESCENS'''<br />
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{{Structure
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|PDB= 1i7q |SIZE=350|CAPTION= <scene name='initialview01'>1i7q</scene>, resolution 1.95&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ILG:GLUTAMYL+GROUP'>ILG</scene>, <scene name='pdbligand=BEZ:BENZOIC+ACID'>BEZ</scene> and <scene name='pdbligand=PYR:PYRUVIC ACID'>PYR</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Anthranilate_synthase Anthranilate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.27 4.1.3.27]
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|GENE=
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}}
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'''ANTHRANILATE SYNTHASE FROM S. MARCESCENS'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1I7Q is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ILG:'>ILG</scene>, <scene name='pdbligand=BEZ:'>BEZ</scene> and <scene name='pdbligand=PYR:'>PYR</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Anthranilate_synthase Anthranilate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.27 4.1.3.27] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I7Q OCA].
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1I7Q is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I7Q OCA].
==Reference==
==Reference==
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The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, L-tryptophan., Spraggon G, Kim C, Nguyen-Huu X, Yee MC, Yanofsky C, Mills SE, Proc Natl Acad Sci U S A. 2001 May 22;98(11):6021-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11371633 11371633]
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The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, L-tryptophan., Spraggon G, Kim C, Nguyen-Huu X, Yee MC, Yanofsky C, Mills SE, Proc Natl Acad Sci U S A. 2001 May 22;98(11):6021-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11371633 11371633]
[[Category: Anthranilate synthase]]
[[Category: Anthranilate synthase]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: glutamyl thioester]]
[[Category: glutamyl thioester]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:08:55 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:46:38 2008''

Revision as of 09:46, 20 March 2008


PDB ID 1i7q

Drag the structure with the mouse to rotate
, resolution 1.95Å
Ligands: , , and
Activity: Anthranilate synthase, with EC number 4.1.3.27
Coordinates: save as pdb, mmCIF, xml



ANTHRANILATE SYNTHASE FROM S. MARCESCENS


Overview

The crystal structure of anthranilate synthase (AS) from Serratia marcescens, a mesophilic bacterium, has been solved in the presence of its substrates, chorismate and glutamine, and one product, glutamate, at 1.95 A, and with its bound feedback inhibitor, tryptophan, at 2.4 A. In comparison with the AS structure from the hyperthermophile Sulfolobus solfataricus, the S. marcescens structure shows similar subunit structures but a markedly different oligomeric organization. One crystal form of the S. marcescens enzyme displays a bound pyruvate as well as a putative anthranilate (the nitrogen group is ambiguous) in the TrpE subunit. It also confirms the presence of a covalently bound glutamyl thioester intermediate in the TrpG subunit. The tryptophan-bound form reveals that the inhibitor binds at a site distinct from that of the substrate, chorismate. Bound tryptophan appears to prevent chorismate binding by a demonstrable conformational effect, and the structure reveals how occupancy of only one of the two feedback inhibition sites can immobilize the catalytic activity of both TrpE subunits. The presence of effectors in the structure provides a view of the locations of some of the amino acid residues in the active sites. Our findings are discussed in terms of the previously described AS structure of S. solfataricus, mutational data obtained from enteric bacteria, and the enzyme's mechanism of action.

About this Structure

1I7Q is a Protein complex structure of sequences from Serratia marcescens. Full crystallographic information is available from OCA.

Reference

The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, L-tryptophan., Spraggon G, Kim C, Nguyen-Huu X, Yee MC, Yanofsky C, Mills SE, Proc Natl Acad Sci U S A. 2001 May 22;98(11):6021-6. PMID:11371633

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