1chr
From Proteopedia
(New page: 200px<br /><applet load="1chr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1chr, resolution 3.0Å" /> '''CRYSTAL STRUCTURE OF ...) |
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caption="1chr, resolution 3.0Å" /> | caption="1chr, resolution 3.0Å" /> | ||
'''CRYSTAL STRUCTURE OF CHLOROMUCONATE CYCLOISOMERASE FROM ALCALIGENES EUTROPHUS JMP134 (PJP4) AT 3 ANGSTROMS RESOLUTION'''<br /> | '''CRYSTAL STRUCTURE OF CHLOROMUCONATE CYCLOISOMERASE FROM ALCALIGENES EUTROPHUS JMP134 (PJP4) AT 3 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Chloromuconate cycloisomerase (E.C. 5.5.1.7) is an enzyme involved in the | + | Chloromuconate cycloisomerase (E.C. 5.5.1.7) is an enzyme involved in the 2,4-dichlorophenoxyacetate degradation pathway of Alcaligenes eutrophus JMP134 (pJP4). The crystal structure of this protein was determined at 3 A resolution by molecular-replacement techniques using atomic coordinates from the reported crystal structure of the homologous muconate cycloisomerase (E.C. 5.5.1.1) from Pseudomonas putida as the search model (42% identical positions in the sequences). Structure refinement by simulated-annealing and restrained least-squares techniques converged at R = 0.195. In the crystals studied, space group I4, the protein is present as two octamers per unit cell with two subunits per asymmetric unit. Each subunit consists of two globular domains, one of which forms an alpha/beta-barrel. Comparison of this structure with that of muconate cycloisomerase reveals the reasons for the altered substrate specificity of chloromuconate cycloisomerase. Marked differences are observed in polarity, accessibility and hydrogen-bonding potential in the channel leading into the active site as well as in the active center itself. |
==About this Structure== | ==About this Structure== | ||
| - | 1CHR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cupriavidus_necator Cupriavidus necator] with MN and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Chloromuconate_cycloisomerase Chloromuconate cycloisomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.5.1.7 5.5.1.7] Full crystallographic information is available from [http:// | + | 1CHR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cupriavidus_necator Cupriavidus necator] with <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Chloromuconate_cycloisomerase Chloromuconate cycloisomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.5.1.7 5.5.1.7] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CHR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Cupriavidus necator]] | [[Category: Cupriavidus necator]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Carrell, H | + | [[Category: Carrell, H L.]] |
| - | [[Category: Glusker, J | + | [[Category: Glusker, J P.]] |
[[Category: Goldman, A.]] | [[Category: Goldman, A.]] | ||
[[Category: Hammer, A.]] | [[Category: Hammer, A.]] | ||
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[[Category: Hoier, H.]] | [[Category: Hoier, H.]] | ||
[[Category: Schloemann, M.]] | [[Category: Schloemann, M.]] | ||
| - | [[Category: Stezowski, J | + | [[Category: Stezowski, J J.]] |
[[Category: CL]] | [[Category: CL]] | ||
[[Category: MN]] | [[Category: MN]] | ||
[[Category: isomerase]] | [[Category: isomerase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:06:18 2008'' |
Revision as of 10:06, 21 February 2008
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CRYSTAL STRUCTURE OF CHLOROMUCONATE CYCLOISOMERASE FROM ALCALIGENES EUTROPHUS JMP134 (PJP4) AT 3 ANGSTROMS RESOLUTION
Overview
Chloromuconate cycloisomerase (E.C. 5.5.1.7) is an enzyme involved in the 2,4-dichlorophenoxyacetate degradation pathway of Alcaligenes eutrophus JMP134 (pJP4). The crystal structure of this protein was determined at 3 A resolution by molecular-replacement techniques using atomic coordinates from the reported crystal structure of the homologous muconate cycloisomerase (E.C. 5.5.1.1) from Pseudomonas putida as the search model (42% identical positions in the sequences). Structure refinement by simulated-annealing and restrained least-squares techniques converged at R = 0.195. In the crystals studied, space group I4, the protein is present as two octamers per unit cell with two subunits per asymmetric unit. Each subunit consists of two globular domains, one of which forms an alpha/beta-barrel. Comparison of this structure with that of muconate cycloisomerase reveals the reasons for the altered substrate specificity of chloromuconate cycloisomerase. Marked differences are observed in polarity, accessibility and hydrogen-bonding potential in the channel leading into the active site as well as in the active center itself.
About this Structure
1CHR is a Single protein structure of sequence from Cupriavidus necator with and as ligands. Active as Chloromuconate cycloisomerase, with EC number 5.5.1.7 Full crystallographic information is available from OCA.
Reference
Crystal structure of chloromuconate cycloisomerase from Alcaligenes eutrophus JMP134 (pJP4) at 3 A resolution., Hoier H, Schlomann M, Hammer A, Glusker JP, Carrell HL, Goldman A, Stezowski JJ, Heinemann U, Acta Crystallogr D Biol Crystallogr. 1994 Jan 1;50(Pt 1):75-84. PMID:15299479
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