Crystal structure of an efficacious gonococcal adherence inhibitor: An enolase from Lactobacillus gasseri
•First structure of enolase from Lactobacillus family, assembles as octamer.•First catalytic loop fully resolved in closed position.•Third catalytic loop disorder suggests high level of flexibility.•Described enolase may conserve putative plasminogen binding motif on catalytic loop. Enolases are hig...
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| Veröffentlicht in: | FEBS Lett 2014-06, Vol.588 (14), p.2212-2216 |
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| creator | Raghunathan, Kannan Harris, Paul T. Spurbeck, Rachel R. Arvidson, Cindy G. Arvidson, Dennis N. |
| description | •First structure of enolase from Lactobacillus family, assembles as octamer.•First catalytic loop fully resolved in closed position.•Third catalytic loop disorder suggests high level of flexibility.•Described enolase may conserve putative plasminogen binding motif on catalytic loop.
Enolases are highly conserved metalloenzymes ubiquitous to cellular metabolism. While these enzymes share a large degree of sequence and structural similarity, they have been shown to possess a wide range of moonlighting functions. Recent studies showed that an enolase from Lactobacillus gasseri impedes the ability of Neisseria gonorrhoeae to adhere to epithelial cells. We present the crystal structure of this enolase, the first from Lactobacillus, with one of its Mg2+ cofactors. Determined using molecular replacement to 2.08Å, the structure has a flexible and surface exposed catalytic loop containing lysines, and may play a role in the inhibitory function.
Eno and enobind by X-ray crystallography (View interaction) |
| doi_str_mv | 10.1016/j.febslet.2014.05.020 |
| format | Article |
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Enolases are highly conserved metalloenzymes ubiquitous to cellular metabolism. While these enzymes share a large degree of sequence and structural similarity, they have been shown to possess a wide range of moonlighting functions. Recent studies showed that an enolase from Lactobacillus gasseri impedes the ability of Neisseria gonorrhoeae to adhere to epithelial cells. We present the crystal structure of this enolase, the first from Lactobacillus, with one of its Mg2+ cofactors. Determined using molecular replacement to 2.08Å, the structure has a flexible and surface exposed catalytic loop containing lysines, and may play a role in the inhibitory function.
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Enolases are highly conserved metalloenzymes ubiquitous to cellular metabolism. While these enzymes share a large degree of sequence and structural similarity, they have been shown to possess a wide range of moonlighting functions. Recent studies showed that an enolase from Lactobacillus gasseri impedes the ability of Neisseria gonorrhoeae to adhere to epithelial cells. We present the crystal structure of this enolase, the first from Lactobacillus, with one of its Mg2+ cofactors. Determined using molecular replacement to 2.08Å, the structure has a flexible and surface exposed catalytic loop containing lysines, and may play a role in the inhibitory function.
Eno and enobind by X-ray crystallography (View interaction)</description><subject>Bacterial Proteins - chemistry</subject><subject>Catalytic Domain</subject><subject>Crystallography, X-Ray</subject><subject>Enolase</subject><subject>Fibronectin</subject><subject>Lactobacillus</subject><subject>Lactobacillus - enzymology</subject><subject>Lactobacillus gasseri</subject><subject>Magnesium - chemistry</subject><subject>Models, Molecular</subject><subject>Moonlighting</subject><subject>Neisseria gonorrhoeae</subject><subject>Phosphopyruvate Hydratase - chemistry</subject><subject>Probiotics</subject><subject>Protein Structure, Quaternary</subject><subject>Protein Structure, Secondary</subject><subject>Structural Homology, Protein</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNksuO1DAQRSMEYpqBTwBFrNgk-JnYbNBMax5ILbEA1pZTKdNupePBTgb13-MoDdthZVk-95arbhXFW0pqSmjz8VA77NKAU80IFTWRNWHkWbGhquUVF416XmxIfqlkq_lF8SqlA8l3RfXL4oIJJTXhalP4bTylyQ5lmuIM0xyxDK60Y4nOebDgw5zKn2EMEAAyZvs9RhwBSz_ufeenED-VVxkfw2ATli6GY7mzMIUui4dhUduUMPrXxQtnh4Rvzudl8eP25vv2vtp9vfuyvdpVIDSRleocNpI1rqUNd4opa5ue885pS6gWHBQBBgJb6GXTdgASNVe9IrkzCk7wy-L96hvS5E0CPyHsIYwjwmQoFYQJlqEPK_QQw68Z02SOPgEOgx0xd2xybUmYJlo8jUquRSslUxmVKwoxpBTRmYfojzaeDCVmSc0czDk1s6RmiDQ5tax7dy4xd0fs_6n-xpSB-xX47Qc8_Z-rub25Zt-WFVg2IPdNuGYyW31erTBn8OgxLiNaAu19XCbUB__Eb_8AB-PAxg</recordid><startdate>20140627</startdate><enddate>20140627</enddate><creator>Raghunathan, Kannan</creator><creator>Harris, Paul T.</creator><creator>Spurbeck, Rachel R.</creator><creator>Arvidson, Cindy G.</creator><creator>Arvidson, Dennis N.</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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>7QL</scope><scope>C1K</scope><scope>OTOTI</scope><orcidid>https://orcid.org/0000-0002-6372-3826</orcidid></search><sort><creationdate>20140627</creationdate><title>Crystal structure of an efficacious gonococcal adherence inhibitor: An enolase from Lactobacillus gasseri</title><author>Raghunathan, Kannan ; Harris, Paul T. ; Spurbeck, Rachel R. ; Arvidson, Cindy G. ; Arvidson, Dennis N.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4905-8bfe6526f7163f828aa6d33bf9a01943c80c2c4e7cd567bcc5e938d808191cf43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Bacterial Proteins - chemistry</topic><topic>Catalytic Domain</topic><topic>Crystallography, X-Ray</topic><topic>Enolase</topic><topic>Fibronectin</topic><topic>Lactobacillus</topic><topic>Lactobacillus - enzymology</topic><topic>Lactobacillus gasseri</topic><topic>Magnesium - chemistry</topic><topic>Models, Molecular</topic><topic>Moonlighting</topic><topic>Neisseria gonorrhoeae</topic><topic>Phosphopyruvate Hydratase - chemistry</topic><topic>Probiotics</topic><topic>Protein Structure, Quaternary</topic><topic>Protein Structure, Secondary</topic><topic>Structural Homology, Protein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Raghunathan, Kannan</creatorcontrib><creatorcontrib>Harris, Paul T.</creatorcontrib><creatorcontrib>Spurbeck, Rachel R.</creatorcontrib><creatorcontrib>Arvidson, Cindy G.</creatorcontrib><creatorcontrib>Arvidson, Dennis N.</creatorcontrib><creatorcontrib>Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>OSTI.GOV</collection><jtitle>FEBS Lett</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Raghunathan, Kannan</au><au>Harris, Paul T.</au><au>Spurbeck, Rachel R.</au><au>Arvidson, Cindy G.</au><au>Arvidson, Dennis N.</au><aucorp>Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystal structure of an efficacious gonococcal adherence inhibitor: An enolase from Lactobacillus gasseri</atitle><jtitle>FEBS Lett</jtitle><addtitle>FEBS Lett</addtitle><date>2014-06-27</date><risdate>2014</risdate><volume>588</volume><issue>14</issue><spage>2212</spage><epage>2216</epage><pages>2212-2216</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>•First structure of enolase from Lactobacillus family, assembles as octamer.•First catalytic loop fully resolved in closed position.•Third catalytic loop disorder suggests high level of flexibility.•Described enolase may conserve putative plasminogen binding motif on catalytic loop.
Enolases are highly conserved metalloenzymes ubiquitous to cellular metabolism. While these enzymes share a large degree of sequence and structural similarity, they have been shown to possess a wide range of moonlighting functions. Recent studies showed that an enolase from Lactobacillus gasseri impedes the ability of Neisseria gonorrhoeae to adhere to epithelial cells. We present the crystal structure of this enolase, the first from Lactobacillus, with one of its Mg2+ cofactors. Determined using molecular replacement to 2.08Å, the structure has a flexible and surface exposed catalytic loop containing lysines, and may play a role in the inhibitory function.
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| subjects | Bacterial Proteins - chemistry Catalytic Domain Crystallography, X-Ray Enolase Fibronectin Lactobacillus Lactobacillus - enzymology Lactobacillus gasseri Magnesium - chemistry Models, Molecular Moonlighting Neisseria gonorrhoeae Phosphopyruvate Hydratase - chemistry Probiotics Protein Structure, Quaternary Protein Structure, Secondary Structural Homology, Protein |
| title | Crystal structure of an efficacious gonococcal adherence inhibitor: An enolase from Lactobacillus gasseri |
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