1GQZ

Refinement of Haemophilus influenzae Diaminopimelate epimerase at 1.7A

Summary for 1GQZ

• Entry DOI: 10.2210/pdb1gqz/pdb
• Related: 1BWZ
• Descriptor: DIAMINOPIMELATE EPIMERASE (2 entities in total)
• Functional Keywords: peptidoglycan biosynthesis, isomerase
• Biological source: HAEMOPHILUS INFLUENZAE
• Cellular location: Cytoplasm : P44859
• Total number of polymer chains: 1
• Total formula weight: 30279.47

Authors

Roper, D.I.,Huyton, T.,Turkenburg, J.P. (deposition date: 2001-12-07, release date: 2003-06-12, Last modification date: 2023-12-13)

Primary citation

Lloyd, A.J.,Huyton, T.,Turkenburg, J.,Roper, D.I.
Refinement of Haemophilus influenzae diaminopimelic acid epimerase (DapF) at 1.75 A resolution suggests a mechanism for stereocontrol during catalysis.
Acta Crystallogr. D Biol. Crystallogr., 60:397-400, 2004

PubMed 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.

PubMed: 14747737
DOI: 10.1107/S0907444903027999

Experimental method

X-RAY DIFFRACTION (1.75 Å)