Toward a structome of Acinetobacter baumannii drug targets.
Acinetobacter baumannii
/ chemistry
Anti-Bacterial Agents
/ pharmacology
Bacterial Proteins
/ antagonists & inhibitors
Coproporphyrinogen Oxidase
/ chemistry
Drug Resistance, Bacterial
/ drug effects
Genome, Bacterial
/ drug effects
Humans
Methionine-tRNA Ligase
/ chemistry
Models, Molecular
Protein Conformation
Uroporphyrinogen Decarboxylase
/ chemistry
X-ray structure
antibiotic resistance
antibiotic targets
gram-negative
structure based drug design
Journal
Protein science : a publication of the Protein Society
ISSN: 1469-896X
Titre abrégé: Protein Sci
Pays: United States
ID NLM: 9211750
Informations de publication
Date de publication:
03 2020
03 2020
Historique:
received:
01
10
2019
revised:
06
01
2020
accepted:
08
01
2020
pubmed:
14
1
2020
medline:
3
2
2021
entrez:
14
1
2020
Statut:
ppublish
Résumé
Acinetobacter baumannii is well known for causing hospital-associated infections due in part to its intrinsic antibiotic resistance as well as its ability to remain viable on surfaces and resist cleaning agents. In a previous publication, A. baumannii strain AB5075 was studied by transposon mutagenesis and 438 essential gene candidates for growth on rich-medium were identified. The Seattle Structural Genomics Center for Infectious Disease entered 342 of these candidate essential genes into our pipeline for structure determination, in which 306 were successfully cloned into expression vectors, 192 were detectably expressed, 165 screened as soluble, 121 were purified, 52 crystalized, 30 provided diffraction data, and 29 structures were deposited in the Protein Data Bank. Here, we report these structures, compare them with human orthologs where applicable, and discuss their potential as drug targets for antibiotic development against A. baumannii.
Identifiants
pubmed: 31930600
doi: 10.1002/pro.3826
pmc: PMC7020997
doi:
Substances chimiques
Anti-Bacterial Agents
0
Bacterial Proteins
0
Coproporphyrinogen Oxidase
EC 1.3.3.3
Uroporphyrinogen Decarboxylase
EC 4.1.1.37
Methionine-tRNA Ligase
EC 6.1.1.10
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
789-802Subventions
Organisme : NIAID NIH HHS
ID : HHSN272201200025C
Pays : United States
Organisme : NIAID NIH HHS
ID : HHSN272201700059C
Pays : United States
Informations de copyright
© 2020 The Protein Society.
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