Lloyd, Adrian J., Huyton, Trevor, Turkenburg, Johan and Roper, David I. (2004) Refinement of Haemophilus influenzae diaminopimelic acid epimerase (DapF) at 1.75 A resolution suggests a mechanism for stereocontrol during catalysis. Acta crystallographica. Section D, Biological crystallography, 60 (2). pp. 397-400. doi:10.1107/S0907444903027999

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Abstract

Diaminopimelate (DAP) epimerase (DapF) is central to the biosynthesis of both lysine and cell-wall peptidoglycan in many bacteria species. The peptidoglycan layer provides great potential for the development of novel antimicrobials as it is a uniquely prokaryotic feature. Crystals of recombinant Haemophilus influenzae DapF that diffract to beyond 2 A resolution have been obtained which facilitated the solution of the structure by molecular replacement at a resolution approximately 1 A higher than that previously determined. An analysis of the structure (i) in comparison to other PLP-independent racemaces and (ii) in relation to the catalytic mechanism and stereospecificity of DapF is presented.

Item Type:	Journal Item
Divisions:	Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- )
Journal or Publication Title:	Acta crystallographica. Section D, Biological crystallography
Publisher:	Wiley
ISSN:	0907-4449
Official Date:	February 2004
Dates:	Date Event February 2004 Published 5 June 2003 Accepted 4 December 2003 Submitted
Volume:	60
Number:	2
Page Range:	pp. 397-400
DOI:	10.1107/S0907444903027999
Status:	Peer Reviewed
Publication Status:	Published
Access rights to Published version:	Restricted or Subscription Access

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