1m32

From Proteopedia

(Difference between revisions)

Revision as of 08:53, 21 April 2021

Crystal Structure of 2-aminoethylphosphonate Transaminase

Structural highlights

1m32 is a 6 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
NonStd Res:
Activity:	2-aminoethylphosphonate--pyruvate transaminase, with EC number 2.6.1.37
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PHNW_SALTY] Involved in phosphonate degradation.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Chen CC, Zhang H, Kim AD, Howard A, Sheldrick GM, Mariano-Dunaway D, Herzberg O. Degradation pathway of the phosphonate ciliatine: crystal structure of 2-aminoethylphosphonate transaminase. Biochemistry. 2002 Nov 5;41(44):13162-9. PMID:12403617

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1m32"

@@ Line 3: / Line 3: @@
 <StructureSection load='1m32' size='340' side='right'caption='[[1m32]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1m32]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M32 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1M32 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1m32]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M32 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=POA:PHOSPHONOACETALDEHYDE'>POA</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=POA:PHOSPHONOACETALDEHYDE'>POA</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/2-aminoethylphosphonate--pyruvate_transaminase 2-aminoethylphosphonate--pyruvate transaminase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.37 2.6.1.37] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m32 OCA], [http://pdbe.org/1m32 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1m32 RCSB], [http://www.ebi.ac.uk/pdbsum/1m32 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1m32 ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1m32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m32 OCA], [https://pdbe.org/1m32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m32 RCSB], [https://www.ebi.ac.uk/pdbsum/1m32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m32 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PHNW_SALTY PHNW_SALTY]] Involved in phosphonate degradation.
+[[https://www.uniprot.org/uniprot/PHNW_SALTY PHNW_SALTY]] Involved in phosphonate degradation.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1m32

From Proteopedia

Revision as of 08:53, 21 April 2021

Crystal Structure of 2-aminoethylphosphonate Transaminase

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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