Cell wall branches, penicillin resistance and the secrets of the MurM protein

被引：29

作者：

Fiser, A

Filipe, SR

Tomasz, A

机构：

[1] Yeshiva Univ Albert Einstein Coll Med, Dept Biochem, Bronx, NY 10461 USA

[2] Yeshiva Univ Albert Einstein Coll Med, Seaver Fdn Ctr Bioinformat, Bronx, NY 10461 USA

[3] Univ Oxford, Dept Biochem, Div Mol Genet, Oxford OX1 3QU, England

[4] Rockefeller Univ, New York, NY 10021 USA

来源：

TRENDS IN MICROBIOLOGY | 2003年 / 11卷 / 12期

关键词：

D O I：

10.1016/j.tim.2003.10.003

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Production of low-affinity forms of penicillin-binding proteins (PBPs), although essential, is not sufficient to protect pneumococci against the inhibitory action of penicillin. Resistance also requires the newly identified protein MurM which, together with MurN, is involved with the synthesis of short peptide branches in the pneumococcal cell wall. Cells in which murM was inactivated produced cell walls without branches and also completely lost penicillin resistance. To understand these surprising observations a 3D-model of MurM was constructed, which helped to put into structural context several of the biochemical and genetic observations made about this protein.

引用

收藏

页码：547 / 553

页数：7

相关论文

共 31 条

[1] Iterated profile searches with PSI-BLAST - a tool for discovery in protein databases [J].

Altschul, SF ;

Koonin, EV .

TRENDS IN BIOCHEMICAL SCIENCES, 1998, 23 (11) :444-447

[2] ConSurf: An algorithmic tool for the identification of functional regions in proteins by surface mapping of phylogenetic information [J].

Armon, A ;

Graur, D ;

Ben-Tal, N .

JOURNAL OF MOLECULAR BIOLOGY, 2001, 307 (01) :447-463

[3] X-ray crystal structure of Staphylococcus aureus FemA [J].

Benson, TE ;

Prince, DB ;

Mutchler, VT ;

Curry, KA ;

Ho, AM ;

Sarver, RW ;

Hagadorn, JC ;

Choi, GH ;

Garlick, RL .

STRUCTURE, 2002, 10 (08) :1107-1115

[4] The Protein Data Bank [J].

Berman, HM ;

Westbrook, J ;

Feng, Z ;

Gilliland, G ;

Bhat, TN ;

Weissig, H ;

Shindyalov, IN ;

Bourne, PE .

NUCLEIC ACIDS RESEARCH, 2000, 28 (01) :235-242

[5] Synthesis of the L-alanyl-L-alanine cross-bridge of Enterococcus faecalis peptidoglycan [J].

Bouhss, A ;

Josseaume, N ;

Severin, A ;

Tabei, K ;

Hugonnet, JE ;

Shlaes, D ;

Mengin-Lecreulx, D ;

van Heijenoort, J ;

Arthur, M .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (48) :45935-45941

[6] Antibiotic resistance as a stress response:: Complete sequencing of a large number of chromosomal loci in Staphylococcus aureus strain COL that impact on the expression of resistance to methicillin [J].

De Lencastre, H ;

Wu, SW ;

Pinho, MG ;

Ludovice, AM ;

Filipe, S ;

Gardete, S ;

Sobral, R ;

Gill, S ;

Chung, M ;

Tomasz, A .

MICROBIAL DRUG RESISTANCE-MECHANISMS EPIDEMIOLOGY AND DISEASE, 1999, 5 (03) :163-175

[7] Specificities of FemA and FemB for different glycine residues: FemB cannot substitute for FemA in Staphylococcal peptidoglycan pentaglycine side chain formation [J].

Ehlert, K ;

Schroder, W ;

Labischinski, H .

JOURNAL OF BACTERIOLOGY, 1997, 179 (23) :7573-7576

[8] Structures of Saccharomyces cerevisiae N-myristoyltransferase with bound myristoylCoA and peptide provide insights about substrate recognition and catalysis [J].

Farazi, TA ;

Waksman, G ;

Gordon, JI .

BIOCHEMISTRY, 2001, 40 (21) :6335-6343

[9]

Filipe SR, 2000, J BIOL CHEM, V275, P27768

[10] Inhibition of the expression of penicillin resistance in Streptococcus pneumoniae by inactivation of cell wall muropeptide branching genes [J].

Filipe, SR ;

Tomasz, A .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (09) :4891-4896

← 1 2 3 4 →