Expression, crystallization and preliminary X-ray crystallographic analysis of cystathionine β-lyase from Acinetobacter baumannii OXA-23
Multidrug‐resistant Acinetobacter baumannii (Ab) has emerged as a leading nosocomial pathogen because of its resistance to most currently available antibiotics. Cystathionine β‐lyase (CBL), a pyridoxal 5′‐phosphate (PLP)‐dependent enzyme, catalyzes the second step in the transsulfuration pathway, wh...
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| Veröffentlicht in: | Acta crystallographica. Section F, Structural biology communications Structural biology communications, 2014-10, Vol.70 (10), p.1368-1371 |
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| container_title | Acta crystallographica. Section F, Structural biology communications |
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| creator | Nguyen, Diem-Quynh Ngo, Ho-Phuong-Thuy Ahn, Yeh-Jin Lee, Sang Hee Kang, Lin-Woo |
| description | Multidrug‐resistant Acinetobacter baumannii (Ab) has emerged as a leading nosocomial pathogen because of its resistance to most currently available antibiotics. Cystathionine β‐lyase (CBL), a pyridoxal 5′‐phosphate (PLP)‐dependent enzyme, catalyzes the second step in the transsulfuration pathway, which is essential for the metabolic interconversion of the sulfur‐containing amino acids homocysteine and methionine. The enzymes of the transsulfuration pathway are considered to be attractive drug targets owing to their specificity to microbes and plants. As a potential target for the development of novel antibacterial drugs, the AbCBL protein was expressed, purified and crystallized. An AbCBL crystal diffracted to 1.57 Å resolution and belonged to the trigonal space group P3112, with unit‐cell parameters a = b = 102.9, c = 136.5 Å. The asymmetric unit contained two monomers, with a corresponding VM of 2.3 Å3 Da−1 and a solvent content of 46.9%. |
| doi_str_mv | 10.1107/S2053230X14017981 |
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Cystathionine β‐lyase (CBL), a pyridoxal 5′‐phosphate (PLP)‐dependent enzyme, catalyzes the second step in the transsulfuration pathway, which is essential for the metabolic interconversion of the sulfur‐containing amino acids homocysteine and methionine. The enzymes of the transsulfuration pathway are considered to be attractive drug targets owing to their specificity to microbes and plants. As a potential target for the development of novel antibacterial drugs, the AbCBL protein was expressed, purified and crystallized. An AbCBL crystal diffracted to 1.57 Å resolution and belonged to the trigonal space group P3112, with unit‐cell parameters a = b = 102.9, c = 136.5 Å. 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Section F, Structural biology communications</title><addtitle>Acta Crystallographica Section F</addtitle><description>Multidrug‐resistant Acinetobacter baumannii (Ab) has emerged as a leading nosocomial pathogen because of its resistance to most currently available antibiotics. Cystathionine β‐lyase (CBL), a pyridoxal 5′‐phosphate (PLP)‐dependent enzyme, catalyzes the second step in the transsulfuration pathway, which is essential for the metabolic interconversion of the sulfur‐containing amino acids homocysteine and methionine. The enzymes of the transsulfuration pathway are considered to be attractive drug targets owing to their specificity to microbes and plants. As a potential target for the development of novel antibacterial drugs, the AbCBL protein was expressed, purified and crystallized. An AbCBL crystal diffracted to 1.57 Å resolution and belonged to the trigonal space group P3112, with unit‐cell parameters a = b = 102.9, c = 136.5 Å. The asymmetric unit contained two monomers, with a corresponding VM of 2.3 Å3 Da−1 and a solvent content of 46.9%.</description><subject>Acinetobacter baumannii - enzymology</subject><subject>Amino Acid Sequence</subject><subject>Bacterial Proteins - biosynthesis</subject><subject>Bacterial Proteins - chemistry</subject><subject>Crystallization</subject><subject>Crystallization Communications</subject><subject>Crystallography, X-Ray</subject><subject>cystathionine β-lyase</subject><subject>Escherichia coli</subject><subject>Gene Expression</subject><subject>Lyases - biosynthesis</subject><subject>Lyases - chemistry</subject><subject>Molecular Sequence Data</subject><subject>multidrug-resistant Acinetobacter baumannii</subject><subject>PLP-dependent enzyme</subject><subject>Pyridoxal Phosphate - chemistry</subject><issn>2053-230X</issn><issn>2053-230X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU9u1DAYxSNERavSA7BBXrIg4D9xbG-QRlWnIFWdxUA7rCzHsTsGJ57aGWi4AdfhIJwJR9OOiliwsvXe7z1_1lcULxB8gxBkb5cYUoIJXKEKIiY4elIcTVI5aU8f3Q-Lk5S-QAinWCafFYeYYl6LCh0VP8_uNtGk5EL_Gug4pkF5736oIQtA9S3Irned61UcwaqMatxT4SaqzdrpjCk_JpdAsEBP3rDOadcb8PtX6UeVDLAxdGCmszaERunBRNCobaf63jmwWM3yoM-LA6t8Mif353HxaX728fR9ebE4_3A6uyg1EbUojbYNtS3UBja2YYLyylQthhaxylBGBWkqUWtlqdXcYMaEUbiqawo156Sl5Lh4t-vdbJvOtNr0Q1RebqLr8h9lUE7-7fRuLW_CN1khziFHueDVfUEMt1uTBtm5pI33qjdhmySqoSCQYywyinaojiGlaOz-GQTltA75zxZz5uXj-faJh51lQOyA786b8f-NcvZ5ji8XFNJpoHKXdWkwd_usil9lzQij8vryXF5dz5eMXS3lkvwB2_K8lw</recordid><startdate>201410</startdate><enddate>201410</enddate><creator>Nguyen, Diem-Quynh</creator><creator>Ngo, Ho-Phuong-Thuy</creator><creator>Ahn, Yeh-Jin</creator><creator>Lee, Sang Hee</creator><creator>Kang, Lin-Woo</creator><general>International Union of Crystallography</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>5PM</scope></search><sort><creationdate>201410</creationdate><title>Expression, crystallization and preliminary X-ray crystallographic analysis of cystathionine β-lyase from Acinetobacter baumannii OXA-23</title><author>Nguyen, Diem-Quynh ; Ngo, Ho-Phuong-Thuy ; Ahn, Yeh-Jin ; Lee, Sang Hee ; Kang, Lin-Woo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3969-ecfb5fd0ce0bfb79584e4d20f174e57593b496caf5fc8e2779ea246650c883d53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Acinetobacter baumannii - enzymology</topic><topic>Amino Acid Sequence</topic><topic>Bacterial Proteins - biosynthesis</topic><topic>Bacterial Proteins - chemistry</topic><topic>Crystallization</topic><topic>Crystallization Communications</topic><topic>Crystallography, X-Ray</topic><topic>cystathionine β-lyase</topic><topic>Escherichia coli</topic><topic>Gene Expression</topic><topic>Lyases - biosynthesis</topic><topic>Lyases - chemistry</topic><topic>Molecular Sequence Data</topic><topic>multidrug-resistant Acinetobacter baumannii</topic><topic>PLP-dependent enzyme</topic><topic>Pyridoxal Phosphate - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nguyen, Diem-Quynh</creatorcontrib><creatorcontrib>Ngo, Ho-Phuong-Thuy</creatorcontrib><creatorcontrib>Ahn, Yeh-Jin</creatorcontrib><creatorcontrib>Lee, Sang Hee</creatorcontrib><creatorcontrib>Kang, Lin-Woo</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>PubMed Central (Full Participant titles)</collection><jtitle>Acta crystallographica. 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An AbCBL crystal diffracted to 1.57 Å resolution and belonged to the trigonal space group P3112, with unit‐cell parameters a = b = 102.9, c = 136.5 Å. The asymmetric unit contained two monomers, with a corresponding VM of 2.3 Å3 Da−1 and a solvent content of 46.9%.</abstract><cop>5 Abbey Square, Chester, Cheshire CH1 2HU, England</cop><pub>International Union of Crystallography</pub><pmid>25286941</pmid><doi>10.1107/S2053230X14017981</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Acinetobacter baumannii - enzymology Amino Acid Sequence Bacterial Proteins - biosynthesis Bacterial Proteins - chemistry Crystallization Crystallization Communications Crystallography, X-Ray cystathionine β-lyase Escherichia coli Gene Expression Lyases - biosynthesis Lyases - chemistry Molecular Sequence Data multidrug-resistant Acinetobacter baumannii PLP-dependent enzyme Pyridoxal Phosphate - chemistry |
| title | Expression, crystallization and preliminary X-ray crystallographic analysis of cystathionine β-lyase from Acinetobacter baumannii OXA-23 |
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