4chi: Difference between revisions
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==(R)-selective amine transaminase from Aspergillus fumigatus at 1.27 A resolution== | ==(R)-selective amine transaminase from Aspergillus fumigatus at 1.27 A resolution== | ||
<StructureSection load='4chi' size='340' side='right' caption='[[4chi]], [[Resolution|resolution]] 1.27Å' scene=''> | <StructureSection load='4chi' size='340' side='right'caption='[[4chi]], [[Resolution|resolution]] 1.27Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4chi]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspfu Aspfu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CHI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CHI FirstGlance]. <br> | <table><tr><td colspan='2'>[[4chi]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspfu Aspfu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CHI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CHI FirstGlance]. <br> | ||
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==See Also== | ==See Also== | ||
*[[Aminotransferase|Aminotransferase]] | *[[Aminotransferase 3D structures|Aminotransferase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Aspfu]] | [[Category: Aspfu]] | ||
[[Category: Large Structures]] | |||
[[Category: Hinrichs, W]] | [[Category: Hinrichs, W]] | ||
[[Category: Palm, G J]] | [[Category: Palm, G J]] | ||
[[Category: Thomsen, M]] | [[Category: Thomsen, M]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 20:46, 14 August 2019
(R)-selective amine transaminase from Aspergillus fumigatus at 1.27 A resolution(R)-selective amine transaminase from Aspergillus fumigatus at 1.27 A resolution
Structural highlights
Publication Abstract from PubMedThe importance of amine transaminases for producing optically pure chiral precursors for pharmaceuticals and chemicals has substantially increased in recent years. The X-ray crystal structure of the (R)-selective amine transaminase from the fungus Aspergillus fumigatus was solved by S-SAD phasing to 1.84 A resolution. The refined structure at 1.27 A resolution provides detailed knowledge about the molecular basis of substrate recognition and conversion to facilitate protein-engineering approaches. The protein forms a homodimer and belongs to fold class IV of the pyridoxal-5'-phosphate-dependent enzymes. Both subunits contribute residues to form two active sites. The structure of the holoenzyme shows the catalytically important cofactor pyridoxal-5'-phosphate bound as an internal aldimine with the catalytically responsible amino-acid residue Lys179, as well as in its free form. A long N-terminal helix is an important feature for the stability of this fungal (R)-selective amine transaminase, but is missing in branched-chain amino-acid aminotransferases and D-amino-acid aminotransferases. Crystallographic characterization of the (R)-selective amine transaminase from Aspergillus fumigatus.,Thomsen M, Skalden L, Palm GJ, Hohne M, Bornscheuer UT, Hinrichs W Acta Crystallogr D Biol Crystallogr. 2014 Apr 1;70(Pt 4):1086-93. doi:, 10.1107/S1399004714001084. Epub 2014 Mar 20. PMID:24699652[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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