1m32
From Proteopedia
(New page: 200px<br /><applet load="1m32" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m32, resolution 2.2Å" /> '''Crystal Structure of ...) |
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| - | [[Image:1m32.gif|left|200px]]<br /><applet load="1m32" size=" | + | [[Image:1m32.gif|left|200px]]<br /><applet load="1m32" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1m32, resolution 2.2Å" /> | caption="1m32, resolution 2.2Å" /> | ||
'''Crystal Structure of 2-aminoethylphosphonate Transaminase'''<br /> | '''Crystal Structure of 2-aminoethylphosphonate Transaminase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Phosphonates allow certain organisms to thrive in otherwise hostile | + | Phosphonates allow certain organisms to thrive in otherwise hostile environments, and 2-aminoethylphosphonate (AEP) is a precursor of many cellular phosphonates. AEP transaminase (AEPT) is an enzyme essential to phosphonate synthesis and degradation pathways. The crystal structure of AEP transaminase was determined by multiwavelength anomalous diffraction of 66 selenium atoms. The refined structure at 2.2 A resolution revealed an overall fold and active site location similar to those of the dimeric, two-domain structure of type I aminotransferases. The active site contains a cofactor, pyridoxal 5'-phosphate (PLP), and the product phosphonoacetaldehyde. Comparison with other type I aminotransferase structures shows that the PLP-protein interactions are conserved. Modeling of bound substrates and products reveals the structural basis for AEP recognition and the stereospecificity of proton elimination at the alpha-carbon and indicates conformational changes along the reaction pathway. |
==About this Structure== | ==About this Structure== | ||
| - | 1M32 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with PO4, PLP and POA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/2-aminoethylphosphonate--pyruvate_transaminase 2-aminoethylphosphonate--pyruvate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.37 2.6.1.37] Full crystallographic information is available from [http:// | + | 1M32 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=PLP:'>PLP</scene> and <scene name='pdbligand=POA:'>POA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/2-aminoethylphosphonate--pyruvate_transaminase 2-aminoethylphosphonate--pyruvate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.37 2.6.1.37] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M32 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Salmonella typhimurium]] | [[Category: Salmonella typhimurium]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Chen, C | + | [[Category: Chen, C C.H.]] |
[[Category: Herzberg, O.]] | [[Category: Herzberg, O.]] | ||
[[Category: Howard, A.]] | [[Category: Howard, A.]] | ||
| - | [[Category: Kim, A | + | [[Category: Kim, A D.]] |
[[Category: Mariano-Dunnaway, D.]] | [[Category: Mariano-Dunnaway, D.]] | ||
| - | [[Category: Sheldrick, G | + | [[Category: Sheldrick, G M.]] |
[[Category: Zhang, H.]] | [[Category: Zhang, H.]] | ||
[[Category: PLP]] | [[Category: PLP]] | ||
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[[Category: plp-dependent aminotransferase fold]] | [[Category: plp-dependent aminotransferase fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:50:56 2008'' |
Revision as of 11:50, 21 February 2008
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Crystal Structure of 2-aminoethylphosphonate Transaminase
Overview
Phosphonates allow certain organisms to thrive in otherwise hostile environments, and 2-aminoethylphosphonate (AEP) is a precursor of many cellular phosphonates. AEP transaminase (AEPT) is an enzyme essential to phosphonate synthesis and degradation pathways. The crystal structure of AEP transaminase was determined by multiwavelength anomalous diffraction of 66 selenium atoms. The refined structure at 2.2 A resolution revealed an overall fold and active site location similar to those of the dimeric, two-domain structure of type I aminotransferases. The active site contains a cofactor, pyridoxal 5'-phosphate (PLP), and the product phosphonoacetaldehyde. Comparison with other type I aminotransferase structures shows that the PLP-protein interactions are conserved. Modeling of bound substrates and products reveals the structural basis for AEP recognition and the stereospecificity of proton elimination at the alpha-carbon and indicates conformational changes along the reaction pathway.
About this Structure
1M32 is a Single protein structure of sequence from Salmonella typhimurium with , and as ligands. Active as 2-aminoethylphosphonate--pyruvate transaminase, with EC number 2.6.1.37 Full crystallographic information is available from OCA.
Reference
Degradation pathway of the phosphonate ciliatine: crystal structure of 2-aminoethylphosphonate transaminase., Chen CC, Zhang H, Kim AD, Howard A, Sheldrick GM, Mariano-Dunaway D, Herzberg O, Biochemistry. 2002 Nov 5;41(44):13162-9. PMID:12403617
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