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1
Disulfide bridges are not involved in penicillin-binding protein 1b dimerization in Escherichia coli.二硫键不参与大肠杆菌中青霉素结合蛋白1b的二聚化过程。
J Bacteriol. 1999 May;181(9):2970-2. doi: 10.1128/JB.181.9.2970-2972.1999.
2
Penicillin-binding proteins 1a and 1b form independent dimers in Escherichia coli.青霉素结合蛋白1a和1b在大肠杆菌中形成独立的二聚体。
J Bacteriol. 2002 Jul;184(13):3749-52. doi: 10.1128/JB.184.13.3749-3752.2002.
3
Differential responses of Escherichia coli cells expressing cytoplasmic domain mutants of penicillin-binding protein 1b after impairment of penicillin-binding proteins 1a and 3.青霉素结合蛋白1a和3受损后,表达青霉素结合蛋白1b胞质结构域突变体的大肠杆菌细胞的差异反应。
J Bacteriol. 2001 Jan;183(1):200-6. doi: 10.1128/JB.183.1.200-206.2001.
4
The catalytic, glycosyl transferase and acyl transferase modules of the cell wall peptidoglycan-polymerizing penicillin-binding protein 1b of Escherichia coli.大肠杆菌细胞壁肽聚糖聚合青霉素结合蛋白1b的催化模块、糖基转移酶模块和酰基转移酶模块。
Mol Microbiol. 1999 Oct;34(2):350-64. doi: 10.1046/j.1365-2958.1999.01612.x.
5
Sequence of the ponA gene and characterization of the penicillin-binding protein 1A of Pseudomonas aeruginosa PAO1.铜绿假单胞菌PAO1的ponA基因序列及青霉素结合蛋白1A的特性分析
Gene. 1997 Oct 15;199(1-2):49-56. doi: 10.1016/s0378-1119(97)00345-4.
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Mutational analysis of the Streptococcus pneumoniae bimodular class A penicillin-binding proteins.肺炎链球菌双模块A类青霉素结合蛋白的突变分析
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7
Differences between inner membrane and peptidoglycan-associated PBP1B dimers of Escherichia coli.大肠杆菌内膜与肽聚糖相关的PBP1B二聚体之间的差异。
J Bacteriol. 1995 Apr;177(7):1860-3. doi: 10.1128/jb.177.7.1860-1863.1995.
8
Identification of a penicillin-binding protein 3 homolog, PBP3x, in Pseudomonas aeruginosa: gene cloning and growth phase-dependent expression.铜绿假单胞菌中青霉素结合蛋白3同源物PBP3x的鉴定:基因克隆及生长阶段依赖性表达
J Bacteriol. 1997 Mar;179(5):1490-6. doi: 10.1128/jb.179.5.1490-1496.1997.
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Hybrid proteins of the transglycosylase and the transpeptidase domains of PBP1B and PBP3 of Escherichia coli.大肠杆菌PBP1B和PBP3的转糖基酶和转肽酶结构域的杂合蛋白。
J Bacteriol. 1995 Nov;177(21):6290-3. doi: 10.1128/jb.177.21.6290-6293.1995.
10
Overproduction of inactive variants of the murein synthase PBP1B causes lysis in Escherichia coli.胞壁质合酶PBP1B的无活性变体过量产生会导致大肠杆菌裂解。
J Bacteriol. 2003 Sep;185(18):5342-8. doi: 10.1128/JB.185.18.5342-5348.2003.

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1
Identification of a stable complex between a [NiFe]-hydrogenase catalytic subunit and its maturation protease.鉴定[NiFe]氢化酶催化亚基与其成熟蛋白酶之间的稳定复合物。
FEBS Lett. 2017 Jan;591(2):338-347. doi: 10.1002/1873-3468.12540. Epub 2017 Jan 11.
2
Identification of Functional Regulatory Residues of the β -Lactam Inducible Penicillin Binding Protein in Methicillin-Resistant Staphylococcus aureus.耐甲氧西林金黄色葡萄球菌中β-内酰胺诱导型青霉素结合蛋白功能调控残基的鉴定
Chemother Res Pract. 2013;2013:614670. doi: 10.1155/2013/614670. Epub 2013 Jul 29.
3
Overproduction of inactive variants of the murein synthase PBP1B causes lysis in Escherichia coli.胞壁质合酶PBP1B的无活性变体过量产生会导致大肠杆菌裂解。
J Bacteriol. 2003 Sep;185(18):5342-8. doi: 10.1128/JB.185.18.5342-5348.2003.
4
Penicillin-binding proteins 1a and 1b form independent dimers in Escherichia coli.青霉素结合蛋白1a和1b在大肠杆菌中形成独立的二聚体。
J Bacteriol. 2002 Jul;184(13):3749-52. doi: 10.1128/JB.184.13.3749-3752.2002.
5
Differential responses of Escherichia coli cells expressing cytoplasmic domain mutants of penicillin-binding protein 1b after impairment of penicillin-binding proteins 1a and 3.青霉素结合蛋白1a和3受损后,表达青霉素结合蛋白1b胞质结构域突变体的大肠杆菌细胞的差异反应。
J Bacteriol. 2001 Jan;183(1):200-6. doi: 10.1128/JB.183.1.200-206.2001.

本文引用的文献

1
Penicillin-binding proteins. Wall peptidoglycan assembly and resistance to penicillin: facts, doubts and hopes.青霉素结合蛋白。细胞壁肽聚糖组装和对青霉素的耐药性:事实、疑问和希望。
Int J Antimicrob Agents. 1997 Feb;8(1):45-60. doi: 10.1016/s0924-8579(96)00358-5.
2
Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli.大肠杆菌承受压力和维持形状的胞壁质囊的生长
Microbiol Mol Biol Rev. 1998 Mar;62(1):181-203. doi: 10.1128/MMBR.62.1.181-203.1998.
3
Morphogenesis of Escherichia coli.大肠杆菌的形态发生
Microbiol Mol Biol Rev. 1998 Mar;62(1):110-29. doi: 10.1128/MMBR.62.1.110-129.1998.
4
Kinship and diversification of bacterial penicillin-binding proteins and beta-lactamases.细菌青霉素结合蛋白和β-内酰胺酶的亲缘关系与多样性
Antimicrob Agents Chemother. 1998 Jan;42(1):1-17. doi: 10.1128/AAC.42.1.1.
5
Topographical and functional investigation of Escherichia coli penicillin-binding protein 1b by alanine stretch scanning mutagenesis.通过丙氨酸延伸扫描诱变对大肠杆菌青霉素结合蛋白1b进行拓扑学和功能研究。
J Bacteriol. 1997 Aug;179(15):4761-7. doi: 10.1128/jb.179.15.4761-4767.1997.
6
Affinity chromatography as a means to study multienzyme complexes involved in murein synthesis.亲和层析作为一种研究参与胞壁质合成的多酶复合物的方法。
Microb Drug Resist. 1996 Spring;2(1):155-7. doi: 10.1089/mdr.1996.2.155.
7
Molecular interplay of murein synthases and murein hydrolases in Escherichia coli.大肠杆菌中胞壁质合成酶与胞壁质水解酶的分子相互作用
Microb Drug Resist. 1996 Spring;2(1):99-103. doi: 10.1089/mdr.1996.2.99.
8
Specific interaction of penicillin-binding proteins 3 and 7/8 with soluble lytic transglycosylase in Escherichia coli.大肠杆菌中青霉素结合蛋白3与7/8和可溶性溶菌转糖基酶的特异性相互作用。
J Biol Chem. 1994 Aug 26;269(34):21603-7.
9
Differences between inner membrane and peptidoglycan-associated PBP1B dimers of Escherichia coli.大肠杆菌内膜与肽聚糖相关的PBP1B二聚体之间的差异。
J Bacteriol. 1995 Apr;177(7):1860-3. doi: 10.1128/jb.177.7.1860-1863.1995.
10
Site-directed mutagenesis of double-stranded DNA by the polymerase chain reaction.通过聚合酶链反应对双链DNA进行定点诱变。
Gene. 1994 Dec 30;151(1-2):119-23. doi: 10.1016/0378-1119(94)90641-6.

二硫键不参与大肠杆菌中青霉素结合蛋白1b的二聚化过程。

Disulfide bridges are not involved in penicillin-binding protein 1b dimerization in Escherichia coli.

作者信息

Chalut C, Remy M H, Masson J M

机构信息

Institut de Pharmacologie et de Biologie Structurale du CNRS, Toulouse, France.

出版信息

J Bacteriol. 1999 May;181(9):2970-2. doi: 10.1128/JB.181.9.2970-2972.1999.

DOI:10.1128/JB.181.9.2970-2972.1999
PMID:10217796
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC93747/
Abstract

PBP1b can be found as a dimer in Escherichia coli. Previous results suggested that dimerization involved the cysteine(s) in an intermolecular disulfide bond. We show that either deletion mutants or a mutant without cysteines is fully active and still binds penicillin and that the latter can also form dimers.

摘要

PBP1b在大肠杆菌中以二聚体形式存在。先前的结果表明,二聚化涉及分子间二硫键中的半胱氨酸。我们发现,缺失突变体或不含半胱氨酸的突变体都具有完全活性,仍能结合青霉素,并且后者也能形成二聚体。