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4ce5

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Revision as of 17:41, 7 September 2022

First crystal structure of an (R)-selective omega-transaminase from Aspergillus terreus

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Retrieved from "http://52.214.119.220/wiki/index.php/4ce5"

@@ Line 3: / Line 3: @@
 <StructureSection load='4ce5' size='340' side='right'caption='[[4ce5]], [[Resolution|resolution]] 1.63&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4ce5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspte Aspte]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CE5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CE5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4ce5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_terreus Aspergillus terreus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CE5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CE5 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PDG:N-({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)-D-GLUTAMIC+ACID'>PDG</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PDG:N-({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)-D-GLUTAMIC+ACID'>PDG</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Branched-chain-amino-acid_transaminase Branched-chain-amino-acid transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.42 2.6.1.42] </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=4ce5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ce5 OCA], [https://pdbe.org/4ce5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ce5 RCSB], [https://www.ebi.ac.uk/pdbsum/4ce5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ce5 ProSAT]</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=4ce5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ce5 OCA], [http://pdbe.org/4ce5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ce5 RCSB], [http://www.ebi.ac.uk/pdbsum/4ce5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ce5 ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[[https://www.uniprot.org/uniprot/Q0C8G1_ASPTN Q0C8G1_ASPTN]]
-Chiral amines are important building blocks for the synthesis of pharmaceutical products, fine chemicals, and agrochemicals. omega-Transaminases are able to directly synthesize enantiopure chiral amines by catalysing the transfer of an amino group from a primary amino donor to a carbonyl acceptor with pyridoxal 5'-phosphate (PLP) as cofactor. In nature, (S)-selective amine transaminases are more abundant than the (R)-selective enzymes, and therefore more information concerning their structures is available. Here, we present the crystal structure of an (R)-omega-transaminase from Aspergillus terreus determined by X-ray crystallography at a resolution of 1.6 A. The structure of the protein is a homodimer that displays the typical class IV fold of PLP-dependent aminotransferases. The PLP-cofactor observed in the structure is present in two states (i) covalently bound to the active site lysine (the internal aldimine form) and (ii) as substrate/product adduct (the external aldimine form) and free lysine. Docking studies revealed that (R)-transaminases follow a dual binding mode, in which the large binding pocket can harbour the bulky substituent of the amine or ketone substrate and the alpha-carboxylate of pyruvate or amino acids, and the small binding pocket accommodates the smaller substituent.
-Crystal Structure of an (R)-Selective omega-Transaminase from Aspergillus terreus.,Lyskowski A, Gruber C, Steinkellner G, Schurmann M, Schwab H, Gruber K, Steiner K PLoS One. 2014 Jan 30;9(1):e87350. doi: 10.1371/journal.pone.0087350. eCollection, 2014 Jan 3. PMID:24498081<ref>PMID:24498081</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4ce5" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Aspte]]
+[[Category: Aspergillus terreus]]
-[[Category: Branched-chain-amino-acid transaminase]]
 [[Category: Large Structures]]
-[[Category: Gruber, C]]
+[[Category: Gruber C]]
-[[Category: Gruber, K]]
+[[Category: Gruber K]]
-[[Category: Lyskowski, A]]
+[[Category: Lyskowski A]]
-[[Category: Schurmann, M]]
+[[Category: Schurmann M]]
-[[Category: Schwab, H]]
+[[Category: Schwab H]]
-[[Category: Steiner, K]]
+[[Category: Steiner K]]
-[[Category: Steinkellner, G]]
+[[Category: Steinkellner G]]
-[[Category: Aminotransferase]]
-[[Category: Chiral amine]]
-[[Category: Enantioselectivity]]
-[[Category: Transamination]]
-[[Category: Transferase]]

4ce5

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Revision as of 17:41, 7 September 2022

First crystal structure of an (R)-selective omega-transaminase from Aspergillus terreus

Structural highlights

Function

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