Ligand size is a major determinant of specificity in periplasmic oxyanion-binding proteins: the 1.2 A resolution crystal structure of Azotobacter vinelandii ModA

Ligand size is a major determinant of specificity in periplasmic oxyanion-binding proteins: the 1.2 A resolution crystal structure of Azotobacter vinelandii ModA

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http://www.wikidata.org/entity/Q27766375
Structure, function, and evolution of bacterial ATP-binding cassette systemsOxyanion binding alters conformation and quaternary structure of the c-terminal domain of the transcriptional regulator mode. Implications for molybdate-dependent regulation, signaling, storage, and transportCrystal structures of the liganded and unliganded nickel-binding protein NikA from Escherichia coliApo and ligand-bound structures of ModA from the archaeonMethanosarcina acetivoransClassification of a Haemophilus influenzae ABC Transporter HI1470/71 through Its Cognate Molybdate Periplasmic Binding Protein, MolACrystallization, data collection and phasing of the molybdate-binding protein of the phytopathogen Xanthomonas axonopodis pv. citri.Small substrate transport and mechanism of a molybdate ATP binding cassette transporter in a lipid environment.Atomic structure of a nitrate-binding protein crucial for photosynthetic productivityPredicting ligand-binding function in families of bacterial receptorsBacterial transport of sulfate, molybdate, and related oxyanions.A molecular basis for tungstate selectivity in prokaryotic ABC transport systems.Tungsten transport protein A (WtpA) in Pyrococcus furiosus: the first member of a new class of tungstate and molybdate transporters.TupA: a tungstate binding protein in the periplasm of Desulfovibrio alaskensis G20.Tungstate Uptake by a highly specific ABC transporter in Eubacterium acidaminophilum.Regulation of V-nitrogenase genes in Anabaena variabilis by RNA processing and by dual repressors.The structure of a cyanobacterial bicarbonate transport protein, CmpA.New insight into the architecture of oxy-anion pocket in unliganded conformation of GAT domains: A MD-simulation study.
P2860

Ligand size is a major determinant of specificity in periplasmic oxyanion-binding proteins: the 1.2 A resolution crystal structure of Azotobacter vinelandii ModA

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http://www.wikidata.org/entity/Q27766375
description
1998 nî lūn-bûn
@nan
1998 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
name
Ligand size is a major determi ...... of Azotobacter vinelandii ModA
@ast
Ligand size is a major determi ...... of Azotobacter vinelandii ModA
@en
Ligand size is a major determi ...... of Azotobacter vinelandii ModA
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type
label
Ligand size is a major determi ...... of Azotobacter vinelandii ModA
@ast
Ligand size is a major determi ...... of Azotobacter vinelandii ModA
@en
Ligand size is a major determi ...... of Azotobacter vinelandii ModA
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prefLabel
Ligand size is a major determi ...... of Azotobacter vinelandii ModA
@ast
Ligand size is a major determi ...... of Azotobacter vinelandii ModA
@en
Ligand size is a major determi ...... of Azotobacter vinelandii ModA
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P1433
P1476
P2093
P304
P31
P356
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P478
P577
P698
P921
P356
P1433
P1476
Ligand size is a major determi ...... of Azotobacter vinelandii ModA
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P2093
P304
P31
P356
10.1016/S0969-2126(98)00151-8
P433
P478
P577
P698
P921