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1ax4
From Proteopedia
(New page: 200px<br /> <applet load="1ax4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ax4, resolution 2.1Å" /> '''TRYPTOPHANASE FROM P...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1AX4 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Proteus_vulgaris Proteus vulgaris]] with K as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.99.1 4.1.99.1]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AX4 OCA]]. | + | 1AX4 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Proteus_vulgaris Proteus vulgaris]] with K as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Lyase Lyase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.99.1 4.1.99.1]]. Structure known Active Sites: LPA, LPB, LPC, LPD, POA, POB, POC and POD. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AX4 OCA]]. |
==Reference== | ==Reference== | ||
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[[Category: tryptophan indole-lyase]] | [[Category: tryptophan indole-lyase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 08:37:19 2007'' |
Revision as of 06:32, 30 October 2007
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TRYPTOPHANASE FROM PROTEUS VULGARIS
Overview
The X-ray structure of tryptophanase (Tnase) reveals the interactions, responsible for binding of the pyridoxal 5'-phosphate (PLP) and atomic, details of the K+ binding site essential for catalysis. The structure of, holo Tnase from Proteus vulgaris (space group P2(1)2(1)2(1) with a = 115.0, A, b = 118.2 A, c = 153.7 A) has been determined at 2.1 A resolution by, molecular replacement using tyrosine phenol-lyase (TPL) coordinates. The, final model of Tnase, refined to an R-factor of 18.7%, (Rfree = 22.8%), suggests that the PLP-enzyme from observed in the structure is a, ketoenamine. PLP is bound in a cleft formed by both the small and large, domains of one subunit and the large domain of the adjacent subunit in the, so-called "catalytic" dimer. The K+ cations are located on the ... [(full description)]
About this Structure
1AX4 is a [Single protein] structure of sequence from [Proteus vulgaris] with K as [ligand]. Active as [Lyase], with EC number [4.1.99.1]. Structure known Active Sites: LPA, LPB, LPC, LPD, POA, POB, POC and POD. Full crystallographic information is available from [OCA].
Reference
Crystal structure of tryptophanase., Isupov MN, Antson AA, Dodson EJ, Dodson GG, Dementieva IS, Zakomirdina LN, Wilson KS, Dauter Z, Lebedev AA, Harutyunyan EH, J Mol Biol. 1998 Feb 27;276(3):603-23. PMID:9551100
Page seeded by OCA on Tue Oct 30 08:37:19 2007
Categories: Proteus vulgaris | Single protein | Antson, A.A. | Dauter, Z. | Dementieva, I.S. | Dodson, E.J. | Dodson, G.G. | Harutyunyan, E.H. | Isupov, M.N. | Lebedev, A.A. | Wilson, K.S. | Zakomirdina, L.N. | K | Monovalent cation binding site | Pyridoxal 5'-phosphate | Tryptophan biosynthesis | Tryptophan indole-lyase
