1bd0

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(New page: 200px<br /> <applet load="1bd0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bd0, resolution 1.6&Aring;" /> '''ALANINE RACEMASE COM...)
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==About this Structure==
==About this Structure==
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1BD0 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]] with IN5 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=5.1.1.1 5.1.1.1]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BD0 OCA]].
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1BD0 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]] with IN5 as [[http://en.wikipedia.org/wiki/ligand ligand]]. 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]]. Structure known Active Site: CIC. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BD0 OCA]].
==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9671513 9671513]
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9671513 9671513]
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[[Category: Alanine racemase]]
[[Category: Geobacillus stearothermophilus]]
[[Category: Geobacillus stearothermophilus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: pyridoxal phosphate]]
[[Category: pyridoxal phosphate]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 18:00:29 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:30:40 2007''

Revision as of 09:25, 30 October 2007


1bd0, resolution 1.6Å

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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 ... [(full description)]

About this Structure

1BD0 is a [Single protein] structure of sequence from [Geobacillus stearothermophilus] with IN5 as [ligand]. Active as [Alanine racemase], with EC number [5.1.1.1]. Structure known Active Site: CIC. 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

Page seeded by OCA on Tue Oct 30 11:30:40 2007

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