Importance of the E-46-D-160 polypeptide segment of the non-penicillin-binding module for the folding of the low-affinity, multimodular class B penicillin-binding protein 5 of Enterococus hirae.

M E Mollerach; P Partoune; J Coyette; J M Ghuysen

首页> 外文期刊>Journal of bacteriology >Importance of the E-46-D-160 polypeptide segment of the non-penicillin-binding module for the folding of the low-affinity, multimodular class B penicillin-binding protein 5 of Enterococus hirae.

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Importance of the E-46-D-160 polypeptide segment of the non-penicillin-binding module for the folding of the low-affinity, multimodular class B penicillin-binding protein 5 of Enterococus hirae.

机译：非青霉素结合模块的E-46-D-160多肽片段对于折叠平肠肠杆菌的低亲和力，多模块B类青霉素结合蛋白5的重要性。

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Compared with the other class B multimodular penicillin- binding proteins (PBPs), the low-affinity PBP5 responsible for penicillin resistance in Enterococcus hirae R40, has an extended non-penicillin-binding module because of the presence of an approximately 110-amino-acid E-46(-)D-160 insert downstream from the membrane anchor. Expression of pbp5 genes lacking various parts of the insert-encoding region gives rise to proteins that are inert in terms of penicillin binding, showing that during folding of the PBP, the insert plays a role in the acquisition of a correct penicillin-binding configuration by the G-364(-)Q-678 carboxy-terminal module.

机译：与其他B类多模块青霉素结合蛋白（PBP）相比，负责平肠肠球菌R40的青霉素耐药性的低亲和力PBP5具有扩展的非青霉素结合模块，因为存在约110个氨基酸E-46（-）D-160插入膜锚的下游。缺少插入序列编码区各个部分的pbp5基因的表达产生了对青霉素结合呈惰性的蛋白质，这表明在PBP折叠期间，该插入物在通过以下方式获得正确的青霉素结合构型中起作用G-364（-）Q-678羧基端模块。

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《Journal of bacteriology》 |1996年第6期|共2页
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M E Mollerach; P Partoune; J Coyette; J M Ghuysen;
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1. The non-penicillin-binding module of the tripartite penicillin-binding protein 3 of Escherichia coli is required for folding and/or stability of the penicillin-binding module and the membrane-anchoring module confers cell septation activity on the folded structure. [J] . C Goffin, C Fraipont, J Ayala, Journal of bacteriology . 1996,第18期

机译：大肠杆菌的三重青霉素结合蛋白3的非青霉素结合模块对于青霉素结合模块的折叠和/或稳定性是必需的，并且膜锚定模块赋予折叠结构上的细胞分离活性。
2. Dual multimodular class A penicillin-binding proteins in Mycobacterium leprae. [J] . S Lepage, P Dubois, T K Ghosh, Journal of bacteriology . 1997,第14期

机译：麻风分枝杆菌中的双重多模块A类青霉素结合蛋白。
3. beta-lactam resistance in Streptococcus pneumoniae: penicillin-binding proteins and non-penicillin-binding proteins. [J] . Hakenbeck R, Grebe T, Zahner D, Molecular Microbiology . 1999,第4期

机译：肺炎链球菌的β-内酰胺耐药性：青霉素结合蛋白和非青霉素结合蛋白。
4. Optimizing aqueous fold stability for short polypeptides:20 residue miniprotein constructs that melt as high as at 61 degC [C] . Niels H.Andersen, Bipasha Barua, R.Matthew Fesinmeyer, the International Peptide Symposium . 2001

机译：优化短多肽的含水折叠稳定性：20个残基MiniPRotein构建体，其熔化高达61 degc
5. Biosensors based on the binding-induced folding of proteins and polypeptides. [D] . Oh, Kenneth Joo-suk. 2007

机译：基于结合诱导的蛋白质和多肽折叠的生物传感器。
6. Importance of the E-46-D-160 polypeptide segment of the non-penicillin-binding module for the folding of the low-affinity multimodular class B penicillin-binding protein 5 of Enterococus hirae. [O] . M E Mollerach, P Partoune, J Coyette, 1996

机译：非青霉素结合模块的E-46-D-160多肽片段对于折叠平肠肠杆菌的低亲和力多模块B类青霉素结合蛋白5的重要性。
7. Importance of the E-46-D-160 polypeptide segment of the non-penicillin-binding module for the folding of the low-affinity, multimodular class B penicillin-binding protein 5 of Enterococus hirae. [O] . Mollerach, M E, Partoune, P, Coyette, J, 1996

机译：非青霉素结合模块的E-46-D-160多肽片段对于折叠平肠肠杆菌的低亲和力，多模块B类青霉素结合蛋白5的重要性。

Importance of the E-46-D-160 polypeptide segment of the non-penicillin-binding module for the folding of the low-affinity, multimodular class B penicillin-binding protein 5 of Enterococus hirae.

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