Purification, crystallization and preliminary X-ray analysis of Escherichia coli UDP-N-acetylmuramoyl:l-alanine ligase (MurC)
UDP‐N‐acetylmuramoyl:l‐alanine ligase (MurC) is involved in the pathway leading from UDP‐N‐glucosamine to the UDP‐N‐acetylmuramoyl:pentapeptide unit, which is the building block for the peptidoglycan layer found in all bacterial cell walls. The pathways leading to the biosynthesis of the peptidoglyc...
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| Veröffentlicht in: | Acta Crystallographica Section D Biological Crystallography 2003-08, Vol.59 (8), p.1510-1513 |
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| creator | Deva, Taru Pryor, KellyAnn D. Leiting, Barbara Baker, Edward N. Smith, Clyde A. |
| description | UDP‐N‐acetylmuramoyl:l‐alanine ligase (MurC) is involved in the pathway leading from UDP‐N‐glucosamine to the UDP‐N‐acetylmuramoyl:pentapeptide unit, which is the building block for the peptidoglycan layer found in all bacterial cell walls. The pathways leading to the biosynthesis of the peptidoglycan layer are important targets for the development of novel antibiotics, since animal cells do not contain these pathways. MurC is the first of four similar ATP‐dependent amide‐bond ligases which share primary and tertiary structural similarities. The crystal structures of three of these have been determined by X‐ray crystallography, giving insights into the binding of the carbohydrate substrate and the ATP. Diffraction‐quality crystals of the enzyme MurC have been obtained in both native and selenomethionine forms and X‐ray diffraction data have been collected at the Se edge at a synchrotron source. The crystals are orthorhombic, with unit‐cell parameters a = 73.9, b = 93.6, c = 176.8 Å, and diffraction has been observed to 2.6 Å resolution. |
| doi_str_mv | 10.1107/S090744490301285X |
| format | Article |
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The pathways leading to the biosynthesis of the peptidoglycan layer are important targets for the development of novel antibiotics, since animal cells do not contain these pathways. MurC is the first of four similar ATP‐dependent amide‐bond ligases which share primary and tertiary structural similarities. The crystal structures of three of these have been determined by X‐ray crystallography, giving insights into the binding of the carbohydrate substrate and the ATP. Diffraction‐quality crystals of the enzyme MurC have been obtained in both native and selenomethionine forms and X‐ray diffraction data have been collected at the Se edge at a synchrotron source. 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D</addtitle><description>UDP‐N‐acetylmuramoyl:l‐alanine ligase (MurC) is involved in the pathway leading from UDP‐N‐glucosamine to the UDP‐N‐acetylmuramoyl:pentapeptide unit, which is the building block for the peptidoglycan layer found in all bacterial cell walls. The pathways leading to the biosynthesis of the peptidoglycan layer are important targets for the development of novel antibiotics, since animal cells do not contain these pathways. MurC is the first of four similar ATP‐dependent amide‐bond ligases which share primary and tertiary structural similarities. The crystal structures of three of these have been determined by X‐ray crystallography, giving insights into the binding of the carbohydrate substrate and the ATP. Diffraction‐quality crystals of the enzyme MurC have been obtained in both native and selenomethionine forms and X‐ray diffraction data have been collected at the Se edge at a synchrotron source. The crystals are orthorhombic, with unit‐cell parameters a = 73.9, b = 93.6, c = 176.8 Å, and diffraction has been observed to 2.6 Å resolution.</description><subject>Adenosine Triphosphate - chemistry</subject><subject>ALANINE-L</subject><subject>amide-bond ligases</subject><subject>Carbohydrates - chemistry</subject><subject>Crystallization</subject><subject>Crystallography, X-Ray</subject><subject>ESCHERICHIA COLI</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli - metabolism</subject><subject>LIGASES</subject><subject>Light</subject><subject>PARTICLE ACCELERATORS</subject><subject>Peptide Synthases - chemistry</subject><subject>Peptide Synthases - isolation & purification</subject><subject>peptoglycan</subject><subject>PURIFICATION</subject><subject>Scattering, Radiation</subject><subject>STANFORD LINEAR ACCELERATOR CENTER</subject><subject>STANFORD SYNCHROTRON RADIATION LABORATORY</subject><subject>SYNCHROTRON RADIATION</subject><subject>UDP-N-acetylmuramoyl:l-alanine ligase</subject><subject>X-Ray Diffraction</subject><subject>X-Rays</subject><issn>1399-0047</issn><issn>0907-4449</issn><issn>1399-0047</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkcFu1DAQhiMEoqXwAFyQuSCQCIxjO7a5LdtSkEpZLa1YuFhe74R1cZLFTgRB4t0JZAVIHDiNNfq-XyP_WXaXwhNKQT59Cxok51wDA1oosbqWHVKmdQ7A5fW_3gfZrZSuAKAomLyZHYywLFmpD7Pviz76yjvb-bZ5TFwcUmdD8N9-LYhtNmQXMfjaNzYOZJVHO4xbG4bkE2krcpLcFqN3W2-Ja4Mnl8eL_Dy3Drsh1H20dTuEZyG3wTa-QRL8R5uQPHzdx_mj29mNyoaEd_bzKLt8cXIxf5mfvTl9NZ-d5Y5TKHKFQjFRKAVSc0kdY1wgwBpL5EqqEkq6WWuspAZRabCbNTpqy1JrJqCglh1l96fcNnXeJOc7dFvXNg26zihGBecj82BidrH93GPqTO2TwzDejW2fjGRcCU2LEaQT6GKbUsTK7KKvx98xFMzPXsw_vYzOvX14v65x88fYFzECagK--IDD_xPN7P3xh5kYGx3VfFJ96vDrb9XGT6aUTArz7vzULCVdLi6Wz82K_QDQNKeJ</recordid><startdate>200308</startdate><enddate>200308</enddate><creator>Deva, Taru</creator><creator>Pryor, KellyAnn D.</creator><creator>Leiting, Barbara</creator><creator>Baker, Edward N.</creator><creator>Smith, Clyde A.</creator><general>Munksgaard International Publishers</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>OTOTI</scope></search><sort><creationdate>200308</creationdate><title>Purification, crystallization and preliminary X-ray analysis of Escherichia coli UDP-N-acetylmuramoyl:l-alanine ligase (MurC)</title><author>Deva, Taru ; Pryor, KellyAnn D. ; Leiting, Barbara ; Baker, Edward N. ; Smith, Clyde A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4102-8e5835288079471c3345e00be6e48786061db9ef7905f90adbec1a669935021a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Adenosine Triphosphate - chemistry</topic><topic>ALANINE-L</topic><topic>amide-bond ligases</topic><topic>Carbohydrates - chemistry</topic><topic>Crystallization</topic><topic>Crystallography, X-Ray</topic><topic>ESCHERICHIA COLI</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli - metabolism</topic><topic>LIGASES</topic><topic>Light</topic><topic>PARTICLE ACCELERATORS</topic><topic>Peptide Synthases - chemistry</topic><topic>Peptide Synthases - isolation & purification</topic><topic>peptoglycan</topic><topic>PURIFICATION</topic><topic>Scattering, Radiation</topic><topic>STANFORD LINEAR ACCELERATOR CENTER</topic><topic>STANFORD SYNCHROTRON RADIATION LABORATORY</topic><topic>SYNCHROTRON RADIATION</topic><topic>UDP-N-acetylmuramoyl:l-alanine ligase</topic><topic>X-Ray Diffraction</topic><topic>X-Rays</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Deva, Taru</creatorcontrib><creatorcontrib>Pryor, KellyAnn D.</creatorcontrib><creatorcontrib>Leiting, Barbara</creatorcontrib><creatorcontrib>Baker, Edward N.</creatorcontrib><creatorcontrib>Smith, Clyde A.</creatorcontrib><creatorcontrib>Stanford Linear Accelerator Center, Menlo Park, CA (US)Stanford Synchrotron Radiation Laboratory (US)</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><jtitle>Acta Crystallographica Section D Biological Crystallography</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Deva, Taru</au><au>Pryor, KellyAnn D.</au><au>Leiting, Barbara</au><au>Baker, Edward N.</au><au>Smith, Clyde A.</au><aucorp>Stanford Linear Accelerator Center, Menlo Park, CA (US)Stanford Synchrotron Radiation Laboratory (US)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification, crystallization and preliminary X-ray analysis of Escherichia coli UDP-N-acetylmuramoyl:l-alanine ligase (MurC)</atitle><jtitle>Acta Crystallographica Section D Biological Crystallography</jtitle><addtitle>Acta Cryst. D</addtitle><date>2003-08</date><risdate>2003</risdate><volume>59</volume><issue>8</issue><spage>1510</spage><epage>1513</epage><pages>1510-1513</pages><issn>1399-0047</issn><issn>0907-4449</issn><eissn>1399-0047</eissn><abstract>UDP‐N‐acetylmuramoyl:l‐alanine ligase (MurC) is involved in the pathway leading from UDP‐N‐glucosamine to the UDP‐N‐acetylmuramoyl:pentapeptide unit, which is the building block for the peptidoglycan layer found in all bacterial cell walls. The pathways leading to the biosynthesis of the peptidoglycan layer are important targets for the development of novel antibiotics, since animal cells do not contain these pathways. MurC is the first of four similar ATP‐dependent amide‐bond ligases which share primary and tertiary structural similarities. The crystal structures of three of these have been determined by X‐ray crystallography, giving insights into the binding of the carbohydrate substrate and the ATP. Diffraction‐quality crystals of the enzyme MurC have been obtained in both native and selenomethionine forms and X‐ray diffraction data have been collected at the Se edge at a synchrotron source. The crystals are orthorhombic, with unit‐cell parameters a = 73.9, b = 93.6, c = 176.8 Å, and diffraction has been observed to 2.6 Å resolution.</abstract><cop>5 Abbey Square, Chester, Cheshire CH1 2HU, England</cop><pub>Munksgaard International Publishers</pub><pmid>12876369</pmid><doi>10.1107/S090744490301285X</doi><tpages>4</tpages></addata></record> |
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| subjects | Adenosine Triphosphate - chemistry ALANINE-L amide-bond ligases Carbohydrates - chemistry Crystallization Crystallography, X-Ray ESCHERICHIA COLI Escherichia coli - enzymology Escherichia coli - metabolism LIGASES Light PARTICLE ACCELERATORS Peptide Synthases - chemistry Peptide Synthases - isolation & purification peptoglycan PURIFICATION Scattering, Radiation STANFORD LINEAR ACCELERATOR CENTER STANFORD SYNCHROTRON RADIATION LABORATORY SYNCHROTRON RADIATION UDP-N-acetylmuramoyl:l-alanine ligase X-Ray Diffraction X-Rays |
| title | Purification, crystallization and preliminary X-ray analysis of Escherichia coli UDP-N-acetylmuramoyl:l-alanine ligase (MurC) |
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