1bd0
From Proteopedia
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|PDB= 1bd0 |SIZE=350|CAPTION= <scene name='initialview01'>1bd0</scene>, resolution 1.6Å | |PDB= 1bd0 |SIZE=350|CAPTION= <scene name='initialview01'>1bd0</scene>, resolution 1.6Å | ||
|SITE= <scene name='pdbsite=CIC:LYS+39+And+TYR+265+(From+The+Other+Subunit)+Are+Proposed+...'>CIC</scene> | |SITE= <scene name='pdbsite=CIC:LYS+39+And+TYR+265+(From+The+Other+Subunit)+Are+Proposed+...'>CIC</scene> | ||
| - | |LIGAND= <scene name='pdbligand=IN5:{1-[(3-HYDROXY-METHYL-5-PHOSPHONOOXY-METHYL-PYRIDIN-4-YLMETHYL)-AMINO]-ETHYL}-PHOSPHONIC ACID'>IN5</scene> | + | |LIGAND= <scene name='pdbligand=IN5:{1-[(3-HYDROXY-METHYL-5-PHOSPHONOOXY-METHYL-PYRIDIN-4-YLMETHYL)-AMINO]-ETHYL}-PHOSPHONIC+ACID'>IN5</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bd0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bd0 OCA], [http://www.ebi.ac.uk/pdbsum/1bd0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bd0 RCSB]</span> | ||
}} | }} | ||
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[[Category: Ringe, D.]] | [[Category: Ringe, D.]] | ||
[[Category: Stamper, G F.]] | [[Category: Stamper, G F.]] | ||
| - | [[Category: IN5]] | ||
[[Category: alanine]] | [[Category: alanine]] | ||
[[Category: alanine phosphonate]] | [[Category: alanine phosphonate]] | ||
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[[Category: pyridoxal phosphate]] | [[Category: pyridoxal phosphate]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:58:23 2008'' |
Revision as of 15:58, 30 March 2008
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| , resolution 1.6Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Alanine racemase, with EC number 5.1.1.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ALANINE RACEMASE COMPLEXED WITH ALANINE PHOSPHONATE
Overview
(R)-1-Aminoethylphosphonic acid (L-Ala-P), a synthetic L-alanine analogue, has antibacterial activity and is a time-dependent inactivator of all purified Gram-positive bacterial alanine racemases that have been tested. L-Ala-P forms an external aldimine with the bound pyridoxal 5'-phosphate (PLP) cofactor, but is neither racemized nor efficiently hydrolyzed. To understand the structural basis of the inactivation of the enzyme by L-Ala-P, we determined the crystal structure of the complex between L-Ala-P and alanine racemase at 1.6 A resolution. The cofactor derivative in the inhibited structure tilts outward from the protein approximately 20 degrees relative to the internal aldimine. The phosphonate oxygens are within hydrogen bonding distance of four amino acid residues and two water molecules in the active site of the enzyme. L-Ala-P is an effective inhibitor of alanine racemase because, upon formation of the external aldimine, the phosphonate group interacts with putative catalytic residues, thereby rendering them unavailable for catalysis. Furthermore, this aldimine appears to be inappropriately aligned for efficient Calpha proton abstraction. The combination of these effects leads to a stable aldimine derivative and potent inactivation of alanine racemase by this compound.
About this Structure
1BD0 is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.
Reference
Reaction of alanine racemase with 1-aminoethylphosphonic acid forms a stable external aldimine., Stamper GF, Morollo AA, Ringe D, Biochemistry. 1998 Jul 21;37(29):10438-45. PMID:9671513
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