1rcq
From Proteopedia
(New page: 200px<br /><applet load="1rcq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rcq, resolution 1.45Å" /> '''The 1.45 A crystal s...) |
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| - | [[Image:1rcq.gif|left|200px]]<br /><applet load="1rcq" size=" | + | [[Image:1rcq.gif|left|200px]]<br /><applet load="1rcq" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rcq, resolution 1.45Å" /> | caption="1rcq, resolution 1.45Å" /> | ||
'''The 1.45 A crystal structure of alanine racemase from a pathogenic bacterium, Pseudomonas aeruginosa, contains both internal and external aldimine forms'''<br /> | '''The 1.45 A crystal structure of alanine racemase from a pathogenic bacterium, Pseudomonas aeruginosa, contains both internal and external aldimine forms'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of the catabolic alanine racemase, DadX, from the pathogenic | + | The structure of the catabolic alanine racemase, DadX, from the pathogenic bacterium Pseudomonas aeruginosa, reported here at 1.45 A resolution, is a dimer in which each monomer is comprised of two domains, an eight-stranded alpha/beta barrel containing the PLP cofactor and a second domain primarily composed of beta-strands. The geometry of each domain is very similar to that of Bacillus stearothermophilus alanine racemase, but the rotation between domains differs by about 15 degrees. This change does not alter the structure of the active site in which almost all residues superimpose well with a low rms difference of 0.86 A. Unexpectedly, the active site of DadX contains a guest substrate that is located where acetate and propionate have been observed in the Bacillus structures. It is modeled as d-lysine and oriented such that its terminal NZ atom makes a covalent bond with C4' of PLP. Since the internal aldimine bond between the protein lysine, Lys33, and C4' of PLP is also unambiguously observed, there appears to be an equilibrium between both internally and externally reacted forms. The PLP cofactor adopts two partially occupied conformational states that resemble previously reported internal and external aldimine complexes. |
==About this Structure== | ==About this Structure== | ||
| - | 1RCQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with PLP and DLY as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alanine_racemase Alanine racemase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.1.1 5.1.1.1] Full crystallographic information is available from [http:// | + | 1RCQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with <scene name='pdbligand=PLP:'>PLP</scene> and <scene name='pdbligand=DLY:'>DLY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alanine_racemase Alanine racemase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.1.1 5.1.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RCQ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Dvorak, A.]] | [[Category: Dvorak, A.]] | ||
[[Category: Im, H.]] | [[Category: Im, H.]] | ||
| - | [[Category: Krause, K | + | [[Category: Krause, K L.]] |
| - | [[Category: Magueres, P | + | [[Category: Magueres, P Le.]] |
[[Category: Strych, U.]] | [[Category: Strych, U.]] | ||
[[Category: DLY]] | [[Category: DLY]] | ||
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[[Category: internal/external aldimine forms]] | [[Category: internal/external aldimine forms]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:49:27 2008'' |
Revision as of 12:49, 21 February 2008
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The 1.45 A crystal structure of alanine racemase from a pathogenic bacterium, Pseudomonas aeruginosa, contains both internal and external aldimine forms
Overview
The structure of the catabolic alanine racemase, DadX, from the pathogenic bacterium Pseudomonas aeruginosa, reported here at 1.45 A resolution, is a dimer in which each monomer is comprised of two domains, an eight-stranded alpha/beta barrel containing the PLP cofactor and a second domain primarily composed of beta-strands. The geometry of each domain is very similar to that of Bacillus stearothermophilus alanine racemase, but the rotation between domains differs by about 15 degrees. This change does not alter the structure of the active site in which almost all residues superimpose well with a low rms difference of 0.86 A. Unexpectedly, the active site of DadX contains a guest substrate that is located where acetate and propionate have been observed in the Bacillus structures. It is modeled as d-lysine and oriented such that its terminal NZ atom makes a covalent bond with C4' of PLP. Since the internal aldimine bond between the protein lysine, Lys33, and C4' of PLP is also unambiguously observed, there appears to be an equilibrium between both internally and externally reacted forms. The PLP cofactor adopts two partially occupied conformational states that resemble previously reported internal and external aldimine complexes.
About this Structure
1RCQ is a Single protein structure of sequence from Pseudomonas aeruginosa with and as ligands. Active as Alanine racemase, with EC number 5.1.1.1 Full crystallographic information is available from OCA.
Reference
Crystal structure at 1.45 A resolution of alanine racemase from a pathogenic bacterium, Pseudomonas aeruginosa, contains both internal and external aldimine forms., LeMagueres P, Im H, Dvorak A, Strych U, Benedik M, Krause KL, Biochemistry. 2003 Dec 23;42(50):14752-61. PMID:14674749
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