| Structural highlights
6bdx is a 1 chain structure with sequence from "diplococcus_gonorrhoeae"_(zopf_1885)_lehmann_and_neumann_1896 "diplococcus gonorrhoeae" (zopf 1885) lehmann and neumann 1896. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | |
| Gene: | dapB, WHOK_00270, WHOK_02229C, WHOM_00688, WHOM_02238C, WHOP_00630, WHOP_02238C, WHOU_00751, WHOU_02311C, WHOV_01184, WHOV_02299C, WHOW_00218, WHOW_02292C, WHOX_00871, WHOX_02228C, WHOY_00570, WHOY_02311C, WHOZ_01787, WHOZ_02300C ("Diplococcus gonorrhoeae" (Zopf 1885) Lehmann and Neumann 1896) |
| Activity: | 4-hydroxy-tetrahydrodipicolinate reductase, with EC number 1.17.1.8 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[A0A1D3EVW8_NEIGO] Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.[HAMAP-Rule:MF_00102][SAAS:SAAS00011094]
Publication Abstract from PubMed
Neisseria gonorrhoeae, an obligate human pathogen, is a leading cause of communicable diseases globally. Due to rapid development of drug resistance, the rate of successfully curing gonococcal infections is rapidly decreasing. Hence, research is being directed toward finding alternative drugs or drug targets to help eradicate these infections. 4-Hydroxy-tetrahydrodipicolinate reductase (DapB), an important enzyme in the meso-diaminopimelate pathway, is a promising target for the development of new antibiotics. This manuscript describes the first structure of DapB from N. gonorrhoeae determined at 1.85A. This enzyme uses NAD(P)H as cofactor. Details of the interactions of the enzyme with its cofactors and a substrate analog/inhibitor are discussed. A large scale bioinformatics analysis of DapBs' sequences is also described.
4-Hydroxy-tetrahydrodipicolinate reductase from Neisseria gonorrhoeae - structure and interactions with coenzymes and substrate analog.,Pote S, Pye SE, Sheahan TE, Gawlicka-Chruszcz A, Majorek KA, Chruszcz M Biochem Biophys Res Commun. 2018 Aug 6. pii: S0006-291X(18)31651-6. doi:, 10.1016/j.bbrc.2018.07.147. PMID:30093108[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pote S, Pye SE, Sheahan TE, Gawlicka-Chruszcz A, Majorek KA, Chruszcz M. 4-Hydroxy-tetrahydrodipicolinate reductase from Neisseria gonorrhoeae - structure and interactions with coenzymes and substrate analog. Biochem Biophys Res Commun. 2018 Aug 6. pii: S0006-291X(18)31651-6. doi:, 10.1016/j.bbrc.2018.07.147. PMID:30093108 doi:http://dx.doi.org/10.1016/j.bbrc.2018.07.147
|
