4chi: Difference between revisions

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'''Unreleased structure'''
==(R)-selective amine transaminase from Aspergillus fumigatus at 1.27 A resolution==
<StructureSection load='4chi' size='340' side='right' caption='[[4chi]], [[Resolution|resolution]] 1.27&Aring;' scene=''>
== Structural highlights ==
[[4chi]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CHI OCA]. <br>
<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
== Publication Abstract from PubMed ==
The 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.


The entry 4chi is ON HOLD  until Paper Publication
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<ref>PMID:24699652</ref>


Authors: Thomsen, M., Palm, G.J., Hinrichs, W.
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
 
== References ==
Description: (R)-selective amine transaminase from Aspergillus fumigatus at 1.27 A resolution
<references/>
__TOC__
</StructureSection>
[[Category: Hinrichs, W.]]
[[Category: Palm, G J.]]
[[Category: Thomsen, M.]]
[[Category: Transferase]]

Revision as of 10:42, 30 April 2014

(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

4chi is a 2 chain structure. Full crystallographic information is available from OCA.

Activity: Glucokinase, with EC number 2.7.1.2

Publication Abstract from PubMed

The 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.

References

  1. Thomsen M, Skalden L, Palm GJ, Hohne M, Bornscheuer UT, Hinrichs W. Crystallographic characterization of the (R)-selective amine transaminase from Aspergillus fumigatus. Acta Crystallogr D Biol Crystallogr. 2014 Apr 1;70(Pt 4):1086-93. doi:, 10.1107/S1399004714001084. Epub 2014 Mar 20. PMID:24699652 doi:http://dx.doi.org/10.1107/S1399004714001084

4chi, resolution 1.27Å

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