4ce5: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==First crystal structure of an (R)-selective omega-transaminase from Aspergillus terreus== | |||
=== | <StructureSection load='4ce5' size='340' side='right' caption='[[4ce5]], [[Resolution|resolution]] 1.63Å' 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> | |||
</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> | |||
<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'>[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://www.rcsb.org/pdb/explore.do?structureId=4ce5 RCSB], [http://www.ebi.ac.uk/pdbsum/4ce5 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Aspte]] | |||
[[Category: Branched-chain-amino-acid transaminase]] | [[Category: Branched-chain-amino-acid transaminase]] | ||
[[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: Aminotransferase]] | ||
[[Category: Chiral amine]] | [[Category: Chiral amine]] | ||
[[Category: Enantioselectivity]] | [[Category: Enantioselectivity]] | ||
[[Category: Transamination | [[Category: Transamination]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 14:02, 4 January 2015
First crystal structure of an (R)-selective omega-transaminase from Aspergillus terreus
| ||||||||||||
