Fine tuning the specificity of the periplasmic phosphate transport receptor. Site-directed mutagenesis, ligand binding, and crystallographic studies
about
Sequence, biophysical, and structural analyses of the PstS lipoprotein (BB0215) fromBorrelia burgdorferireveal a likely binding component of an ABC-type phosphate transporterThe PhoBR two-component system regulates antibiotic biosynthesis in Serratia in response to phosphate.Preliminary time-of-flight neutron diffraction studies of Escherichia coli ABC transport receptor phosphate-binding protein at the Protein Crystallography Station.Crystallization and preliminary X-ray diffraction analysis of the phosphate-binding protein PhoX from Xanthomonas citriAtomic structure of a nitrate-binding protein crucial for photosynthetic productivityThe change of protein intradomain mobility on ligand binding: is it a commonly observed phenomenon?Mycobacterium tuberculosis Phosphate Uptake System Component PstA2 Is Not Required for Gene Regulation or VirulenceA continuous spectrophotometric enzyme-coupled assay for deoxynucleoside triphosphate triphosphohydrolasesA novel analytical method for in vivo phosphate trackingNegative electrostatic surface potential of protein sites specific for anionic ligandsDominant role of local dipolar interactions in phosphate binding to a receptor cleft with an electronegative charge surface: equilibrium, kinetic, and crystallographic studies.Mechanisms of protein-ligand association and its modulation by protein mutations.Crystallization and preliminary X-ray crystallographic analysis of the 38-kDa immunodominant antigen of Mycobacterium tuberculosis.Open Conformation of the Escherichia coli Periplasmic Murein Tripeptide Binding Protein, MppA, at High Resolution.
P2860
Q27680836-FDDF8A50-2032-407B-9F3C-7786E15EE357Q33454972-1D6F1110-4A53-49DC-88AC-BAD78B50E8BBQ33733729-904751B7-D7CB-47C3-9359-E29682F0B4A3Q34652811-5F8F7F11-872E-402C-BC3C-C095BE4D3855Q34772837-7A3B32B4-62DD-47CB-B4DF-FABDA8CB8347Q35051985-B2BB7FA9-0946-491D-80F0-8A4116957371Q36111582-5506FAF1-E0B4-4086-88E3-C87C6908F813Q36553774-EEF0DA00-C440-42B0-A6F4-19C45A76ABA3Q37356238-407F1A0B-7E75-47BA-8CF7-5E2742AB4F15Q37543420-F7F9F8AB-80C3-4275-BE89-92AB284E3EE7Q42117138-38EA4F78-FA7F-45B6-861A-5AC067E2A130Q42584828-02180C13-7763-473F-9B64-8E00C9C44588Q42844003-1D528773-4802-434F-91CB-AC99480AA06EQ55399024-C389AAFA-8F0E-4B2C-A956-EA4B8CDDAE82
P2860
Fine tuning the specificity of the periplasmic phosphate transport receptor. Site-directed mutagenesis, ligand binding, and crystallographic studies
description
1994 nî lūn-bûn
@nan
1994 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Fine tuning the specificity of ...... , and crystallographic studies
@ast
Fine tuning the specificity of ...... , and crystallographic studies
@en
Fine tuning the specificity of ...... , and crystallographic studies
@nl
type
label
Fine tuning the specificity of ...... , and crystallographic studies
@ast
Fine tuning the specificity of ...... , and crystallographic studies
@en
Fine tuning the specificity of ...... , and crystallographic studies
@nl
prefLabel
Fine tuning the specificity of ...... , and crystallographic studies
@ast
Fine tuning the specificity of ...... , and crystallographic studies
@en
Fine tuning the specificity of ...... , and crystallographic studies
@nl
P2093
P3181
P356
P1476
Fine tuning the specificity of ...... , and crystallographic studies
@en
P2093
A Choudhary
F A Quiocho
P S Ledvina
P304
P3181
P356
10.2210/PDB1PBP/PDB
P407
P577
1994-10-07T00:00:00Z