1i7s
From Proteopedia
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'''ANTHRANILATE SYNTHASE FROM SERRATIA MARCESCENS IN COMPLEX WITH ITS END PRODUCT INHIBITOR L-TRYPTOPHAN''' | '''ANTHRANILATE SYNTHASE FROM SERRATIA MARCESCENS IN COMPLEX WITH ITS END PRODUCT INHIBITOR L-TRYPTOPHAN''' | ||
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[[Category: Yanofsky, C.]] | [[Category: Yanofsky, C.]] | ||
[[Category: Yee, M C.]] | [[Category: Yee, M C.]] | ||
| - | [[Category: | + | [[Category: Anthranilate synthase]] |
| - | [[Category: | + | [[Category: Conformational change]] |
| - | [[Category: | + | [[Category: End product inhibition]] |
| - | [[Category: | + | [[Category: Tryptophan binding]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:40:48 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 16:40, 2 May 2008
ANTHRANILATE SYNTHASE FROM SERRATIA MARCESCENS IN COMPLEX WITH ITS END PRODUCT INHIBITOR L-TRYPTOPHAN
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
1I7S 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 Page seeded by OCA on Fri May 2 19:40:48 2008
