2oqx
From Proteopedia
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|PDB= 2oqx |SIZE=350|CAPTION= <scene name='initialview01'>2oqx</scene>, resolution 1.900Å | |PDB= 2oqx |SIZE=350|CAPTION= <scene name='initialview01'>2oqx</scene>, resolution 1.900Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Tryptophanase Tryptophanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.99.1 4.1.99.1] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Tryptophanase Tryptophanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.99.1 4.1.99.1] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ax4|1AX4]], [[2c44|2C44]], [[1tpl|1TPL]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2oqx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oqx OCA], [http://www.ebi.ac.uk/pdbsum/2oqx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2oqx RCSB]</span> | ||
}} | }} | ||
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[[Category: Kogan, A.]] | [[Category: Kogan, A.]] | ||
[[Category: Parola, A.]] | [[Category: Parola, A.]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: EPE]] | ||
| - | [[Category: MG]] | ||
[[Category: lyase]] | [[Category: lyase]] | ||
[[Category: pyridoxal phosphate]] | [[Category: pyridoxal phosphate]] | ||
[[Category: tryptophan catabolism]] | [[Category: tryptophan catabolism]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:21:51 2008'' |
Revision as of 01:21, 31 March 2008
| |||||||
| , resolution 1.900Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Activity: | Tryptophanase, with EC number 4.1.99.1 | ||||||
| Related: | 1AX4, 2C44, 1TPL
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of the apo form of E. coli tryptophanase at 1.9 A resolution
Overview
The crystal structure of apo tryptophanase from Escherichia coli (space group F222, unit-cell parameters a = 118.4, b = 120.1, c = 171.2 A) was determined at 1.9 A resolution using the molecular-replacement method and refined to an R factor of 20.3% (R(free) = 23.2%). The structure revealed a significant shift in the relative orientation of the domains compared with both the holo form of Proteus vulgaris tryptophanase and with another crystal structure of apo E. coli tryptophanase, reflecting the internal flexibility of the molecule. Domain shifts were previously observed in tryptophanase and in the closely related enzyme tyrosine phenol-lyase, with the holo form found in an open conformation and the apo form in either an open or a closed conformation. Here, a wide-open conformation of the apo form of tryptophanase is reported. A conformational change is also observed in loop 297-303. The structure contains a hydrated Mg(2+) at the cation-binding site and a Cl(-) ion at the subunit interface. The enzyme activity depends on the nature of the bound cation, with smaller ions serving as inhibitors. It is hypothesized that this effect arises from variations of the coordination geometry of the bound cation.
About this Structure
2OQX is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The structure of apo tryptophanase from Escherichia coli reveals a wide-open conformation., Tsesin N, Kogan A, Gdalevsky GY, Himanen JP, Cohen-Luria R, Parola AH, Goldgur Y, Almog O, Acta Crystallogr D Biol Crystallogr. 2007 Sep;63(Pt 9):969-74. Epub 2007, Aug 17. PMID:17704565
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