-
Tytuł:
-
Crystal structure of the cytokinin-producing enzyme "lonely guy" (LOG) from Mycobacterium tuberculosis.
-
Autorzy:
-
Shang L; National Clinical Research Center for Infectious Diseases, Guangdong Provincial Clinical Research Center for Tuberculosis, Shenzhen Third People's Hospital, Southern University of Science and Technology, Shenzhen, 518112, China.
Li G; National Clinical Research Center for Infectious Diseases, Guangdong Provincial Clinical Research Center for Tuberculosis, Shenzhen Third People's Hospital, Southern University of Science and Technology, Shenzhen, 518112, China.
Lin Q; Department of Traditional Chinese Medicine, The Baoan People's Hospital of Shenzhen, Shenzhen University, Shenzhen, 518101, China.
Ou M; National Clinical Research Center for Infectious Diseases, Guangdong Provincial Clinical Research Center for Tuberculosis, Shenzhen Third People's Hospital, Southern University of Science and Technology, Shenzhen, 518112, China.
Liang J; National Clinical Research Center for Infectious Diseases, Guangdong Provincial Clinical Research Center for Tuberculosis, Shenzhen Third People's Hospital, Southern University of Science and Technology, Shenzhen, 518112, China.
Xiao G; National Clinical Research Center for Infectious Diseases, Guangdong Provincial Clinical Research Center for Tuberculosis, Shenzhen Third People's Hospital, Southern University of Science and Technology, Shenzhen, 518112, China.
Wang Z; National Clinical Research Center for Infectious Diseases, Guangdong Provincial Clinical Research Center for Tuberculosis, Shenzhen Third People's Hospital, Southern University of Science and Technology, Shenzhen, 518112, China.
Cui S; Institute of Pathogen Biology, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, 100730, China.
Zhang T; State Key Laboratory of Respiratory Disease, Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou, 510700, China.
Liu L; National Clinical Research Center for Infectious Diseases, Guangdong Provincial Clinical Research Center for Tuberculosis, Shenzhen Third People's Hospital, Southern University of Science and Technology, Shenzhen, 518112, China.
Zhang G; National Clinical Research Center for Infectious Diseases, Guangdong Provincial Clinical Research Center for Tuberculosis, Shenzhen Third People's Hospital, Southern University of Science and Technology, Shenzhen, 518112, China. Electronic address: .
-
Źródło:
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2022 Apr 02; Vol. 598, pp. 113-118. Date of Electronic Publication: 2022 Feb 03.
-
Typ publikacji:
-
Journal Article; Research Support, Non-U.S. Gov't
-
Język:
-
English
-
Imprint Name(s):
-
Publication: <2002- >: San Diego, CA : Elsevier
Original Publication: New York, Academic Press.
-
MeSH Terms:
-
Bacterial Proteins/*chemistry
Mycobacterium tuberculosis/*chemistry
Arginine ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Binding Sites ; Crystallography, X-Ray ; Cytokinins/metabolism ; Models, Molecular ; Mycobacterium tuberculosis/genetics ; Protein Conformation ; Protein Multimerization
-
Contributed Indexing:
-
Keywords: Cytokinin; LOG; Mycobacterium tuberculosis
-
Substance Nomenclature:
-
0 (Bacterial Proteins)
0 (Cytokinins)
94ZLA3W45F (Arginine)
-
Entry Date(s):
-
Date Created: 20220214 Date Completed: 20220315 Latest Revision: 20220315
-
Update Code:
-
20240105
-
DOI:
-
10.1016/j.bbrc.2022.01.103
-
PMID:
-
35158209
-
Mycobacterium tuberculosis (Mtb) is an extremely successful intracellular pathogen that cause a large number of death worldwide. It is interesting that this non-phytopathogen can synthesize cytokinin by "lonely guy" (LOG) protein. The cytokinin biosynthesis pathway in Mtb is not clear. Here we determined the crystal structure of LOG from Mtb (MtLOG) at a high resolution of 1.8 Å. MtLOG exists as dimer which belongs to type-I LOG and shows a typical α-β Rossmann fold. Like other LOGs, MtLOG also contains a conserved "PGGXGTXXE" motif that contributes to the formation of an active site. For the first time, we found that the MtLOG binds to Mg 2+ in the negative potential pocket. According to the docking result, we found that Arg78, Arg98 and Tyr162 should be the key amino acid involved in substrate binding. Our findings provide a structural basis for cytokinin study in Mtb and will play an important role in design and development of enzyme inhibitors.
(Copyright © 2022 Elsevier Inc. All rights reserved.)