Crystal structure of D‐glycero‐Β‐D‐manno‐heptose‐1‐phosphate adenylyltransferase from Burkholderia pseudomallei. Issue 1 (31st October 2017)

• Record Type: Journal Article
• Authors: Park, Jimin; Kim, Hyojin; Kim, Suwon; Lee, Daeun; Kim, Mi‐Sun; Shin, Dong Hae
• Is Part Of: Proteins. Volume 86:Issue 1(2018)
• Page Start: 124
• Page End: 131
• Publication Date: 2017-10-31
• Subjects: heptose biosynthesis pathway -- HldC -- lipopolysaccharide -- melioidosis -- nucleotidyltransferase; Proteins -- Periodicals; Proteins -- Periodicals; 572.6
• DOI: 10.1002/prot.25398
• Languages: English
• ISSNs: 0887-3585

Abstract

Abstract: The crystal structure of HldC from B. pseudomallei ( Bp HldC), the fourth enzyme of the heptose biosynthesis pathway, has been determined. Bp HldC converts ATP andd ‐ glycero ‐β‐d ‐ manno ‐heptose‐1‐phosphate into ADP‐d ‐ glycero ‐β‐d ‐ manno ‐heptose and pyrophosphate. The crystal structure of Bp HldC belongs to the nucleotidyltransferase α/β phosphodiesterase superfamily sharing a common Rossmann‐like α/β fold with a conserved T/HXGH sequence motif. The invariant catalytic key residues of Bp HldC indicate that the core catalytic mechanism of Bp HldC may be similar to that of other closest homologues. Intriguingly, a reorientation of the C‐terminal helix seems to guide open and close states of the active site for the catalytic reaction.