Crystal Structures of Active Fully Assembled Substrate- and Product-Bound Complexes of UDP-<i>N</i>-Acetylmuramic Acid:<scp>l</scp>-Alanine Ligase (MurC) from<i>Haemophilus influenzae</i>

Mol, Clifford D.; Brooun, Alexei; Dougan, D.R.; Hilgers, M.T.; Tari, Leslie W.; Wijnands, Robert A.; Knuth, Mark W.; McRee, Duncan E.; Swanson, Ronald V.

doi:10.1128/jb.185.14.4152-4162.2003

Cited by 65 publications

(67 citation statements)

References 37 publications

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“…The Joint Center for Structural Genomics has recently determined the crystal structure of Psychrobacter arcticum Mpl (Protein Data Bank accession no. 3HN7), highlighting the previously noted relationship with MurC enzymes (177). P. arcticum Mpl shows relatively high sequence conservation with Acinetobacter Mpl proteins (56% sequence identity).…”

Section: Peptidoglycan Recycling and Response To ␤-Lactam Antibioticsmentioning

confidence: 68%

Essential Biological Processes of an Emerging Pathogen: DNA Replication, Transcription, and Cell Division in Acinetobacter spp

Robinson

Brzoska

Turner

et al. 2010

Microbiol Mol Biol Rev

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SUMMARY Within the last 15 years, members of the bacterial genus Acinetobacter have risen from relative obscurity to be among the most important sources of hospital-acquired infections. The driving force for this has been the remarkable ability of these organisms to acquire antibiotic resistance determinants, with some strains now showing resistance to every antibiotic in clinical use. There is an urgent need for new antibacterial compounds to combat the threat imposed by Acinetobacter spp. and other intractable bacterial pathogens. The essential processes of chromosomal DNA replication, transcription, and cell division are attractive targets for the rational design of antimicrobial drugs. The goal of this review is to examine the wealth of genome sequence and gene knockout data now available for Acinetobacter spp., highlighting those aspects of essential systems that are most suitable as drug targets. Acinetobacter spp. show several key differences from other pathogenic gammaproteobacteria, particularly in global stress response pathways. The involvement of these pathways in short- and long-term antibiotic survival suggests that Acinetobacter spp. cope with antibiotic-induced stress differently from other microorganisms.

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Section: Peptidoglycan Recycling and Response To ␤-Lactam Antibioticsmentioning

confidence: 68%

Essential Biological Processes of an Emerging Pathogen: DNA Replication, Transcription, and Cell Division in Acinetobacter spp

Robinson

Brzoska

Turner

et al. 2010

Microbiol Mol Biol Rev

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“…Both active sites of the enzyme were localized in the amino-terminal region of CphA; furthermore, five additional conserved stretches with unknown functions were identified in the carboxy-terminal regions of all cyanobacterial CphA proteins (18). The first four conserved regions also exhibited high similarities to those of noncyanobacterial cyanophycin synthetases and to members of the Mur ligase superfamily, including folyl-␥-glutamate ligase (34).…”

mentioning

confidence: 80%

Engineered Cyanophycin Synthetase (CphA) from Nostoc ellipsosporum Confers Enhanced CphA Activity and Cyanophycin Accumulation to Escherichia coli

Hải

Frey

Steinbüchel

2006

Appl Environ Microbiol

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“…Therefore, as expected, MϪ/Ϫ.SAA macrophages failed to survive or proliferate in response to CSF-1 (data not shown). Furthermore, it has been shown in activated c-Kit that after ATPbinding, Cys-672 of the ATP-binding domain (equivalent to Cys-664 of the CSF-1R) forms hydrogen bonds with the adenine N1 atom of ADP (61). It is therefore likely that the SAA mutation distorted the structure of the ATP-binding domain, affecting the ATP binding and/or kinase activation required for receptor tyrosine phosphorylation and consequently for the conformational change in the major kinase domain.…”

Section: Discussionmentioning

confidence: 99%

A CSF-1 Receptor Phosphotyrosine 559 Signaling Pathway Regulates Receptor Ubiquitination and Tyrosine Phosphorylation

Xiong

Song

Cai

et al. 2011

Journal of Biological Chemistry

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Receptor tyrosine kinase (RTK) activation involves ligandinduced receptor dimerization and transphosphorylation on tyrosine residues. Colony-stimulating factor-1 (CSF-1)-induced CSF-1 receptor (CSF-1R) tyrosine phosphorylation and ubiquitination were studied in mouse macrophages. Phosphorylation of CSF-1R Tyr-559, required for the binding of Src family kinases (SFKs), was both necessary and sufficient for these responses and for c-Cbl tyrosine phosphorylation and all three responses were inhibited by SFK inhibitors. In c-Cbldeficient macrophages, CSF-1R ubiquitination and tyrosine phosphorylation were substantially inhibited. Reconstitution with wild-type, but not ubiquitin ligase-defective C381A c-Cbl rescued these responses, while expression of C381A c-Cbl in wild-type macrophages suppressed them. Analysis of site-directed mutations in the CSF-1R further suggests that activated c-Cbl-mediated CSF-1R ubiquitination is required for a conformational change in the major kinase domain that allows amplification of receptor tyrosine phosphorylation and full receptor activation. Thus the results indicate that CSF-1-mediated receptor dimerization leads to a Tyr-559/SFK/c-Cbl pathway resulting in receptor ubiquitination that permits full receptor tyrosine phosphorylation of this class III RTK in macrophages.

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Crystal Structures of Active Fully Assembled Substrate- and Product-Bound Complexes of UDP-N-Acetylmuramic Acid:l-Alanine Ligase (MurC) fromHaemophilus influenzae

Cited by 65 publications

References 37 publications

Essential Biological Processes of an Emerging Pathogen: DNA Replication, Transcription, and Cell Division in Acinetobacter spp

Essential Biological Processes of an Emerging Pathogen: DNA Replication, Transcription, and Cell Division in Acinetobacter spp

Engineered Cyanophycin Synthetase (CphA) from Nostoc ellipsosporum Confers Enhanced CphA Activity and Cyanophycin Accumulation to Escherichia coli

A CSF-1 Receptor Phosphotyrosine 559 Signaling Pathway Regulates Receptor Ubiquitination and Tyrosine Phosphorylation

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