MagC is a NplC/P60‐like member of the α‐2‐macroglobulin Mag complex of Pseudomonas aeruginosa that interacts with peptidoglycan
Bacterial α‐2 macroglobulins (A2Ms) structurally resemble the large spectrum protease inhibitors of the eukaryotic immune system. In Pseudomonas aeruginosa, MagD acts as an A2M and is expressed within a six‐gene operon encoding the MagA‐F proteins. In this work, we employ isothermal calorimetry (ITC...
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| Veröffentlicht in: | FEBS letters 2021-08, Vol.595 (15), p.2034-2046 |
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| container_title | FEBS letters |
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| creator | Zouhir, Samira Contreras‐Martel, Carlos Maragno Trindade, Daniel Attrée, Ina Dessen, Andréa Macheboeuf, Pauline |
| description | Bacterial α‐2 macroglobulins (A2Ms) structurally resemble the large spectrum protease inhibitors of the eukaryotic immune system. In Pseudomonas aeruginosa, MagD acts as an A2M and is expressed within a six‐gene operon encoding the MagA‐F proteins. In this work, we employ isothermal calorimetry (ITC), analytical ultracentrifugation (AUC), and X‐ray crystallography to investigate the function of MagC and show that MagC associates with the macroglobulin complex and with the peptidoglycan (PG). However, the catalytic residues of MagC display an inactive conformation that could suggest that it binds to PG but does not degrade it. We hypothesize that MagC could serve as an anchor between the MagD macroglobulin and the PG and could provide stabilization and/or regulation for the entire complex. |
| doi_str_mv | 10.1002/1873-3468.14148 |
| format | Article |
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In Pseudomonas aeruginosa, MagD acts as an A2M and is expressed within a six‐gene operon encoding the MagA‐F proteins. In this work, we employ isothermal calorimetry (ITC), analytical ultracentrifugation (AUC), and X‐ray crystallography to investigate the function of MagC and show that MagC associates with the macroglobulin complex and with the peptidoglycan (PG). However, the catalytic residues of MagC display an inactive conformation that could suggest that it binds to PG but does not degrade it. We hypothesize that MagC could serve as an anchor between the MagD macroglobulin and the PG and could provide stabilization and/or regulation for the entire complex.</description><subject>Bacteriology</subject><subject>Biochemistry, Molecular Biology</subject><subject>Life Sciences</subject><subject>Microbiology and Parasitology</subject><subject>Molecular biology</subject><subject>NlpC/P60</subject><subject>peptidoglycan hydrolase</subject><subject>α‐2‐macroglobulin</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><recordid>eNqFkbGO1DAQhi0EEstBTesSityO7diblMfqjkNa4Aqordlksmtw4hAnd2xHRc2r8CI8BE-CQ9C1FCNrfn3_L41_xp4LOBcAci2KjcpUbopzkYu8eMBW98pDtgIQeaY3pXrMnsT4CdJeiHLFvr_Fw5a7yJG_6_12fWPg97cf3n0m3lK7p4GHho9H4r9-Jl2mabEawsGH_eRdx5OdV6HtPX2dyZtIUx3a0GFKpGE6uC5ETAE4cteNNGA1Rn7nxiPvqR9dnZJOFXZP2aMGfaRn_94z9vHq8sP2Otu9f_1me7HLKlWaIsNaC6mxbBRIQ7SXoEmYuqlNo0hVeVFLKpUkQgEN5EaVGlFCs6-0SQdLdcZeLrlH9LYfXIvDyQZ09vpiZ2cNlNwoA_pWJPbFwvZD-DJRHG3rYkXeY0dhilbqHLSEUuqErhc0fU2MAzX32QLs3I6du7BzF_ZvO8lhFsed83T6H26vLl_JxfgH5CWU9Q</recordid><startdate>202108</startdate><enddate>202108</enddate><creator>Zouhir, Samira</creator><creator>Contreras‐Martel, Carlos</creator><creator>Maragno Trindade, Daniel</creator><creator>Attrée, Ina</creator><creator>Dessen, Andréa</creator><creator>Macheboeuf, Pauline</creator><general>Wiley</general><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0003-4523-9923</orcidid><orcidid>https://orcid.org/0000-0001-6487-4020</orcidid><orcidid>https://orcid.org/0000-0002-2580-764X</orcidid></search><sort><creationdate>202108</creationdate><title>MagC is a NplC/P60‐like member of the α‐2‐macroglobulin Mag complex of Pseudomonas aeruginosa that interacts with peptidoglycan</title><author>Zouhir, Samira ; Contreras‐Martel, Carlos ; Maragno Trindade, Daniel ; Attrée, Ina ; Dessen, Andréa ; Macheboeuf, Pauline</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3968-ad5125a9f3026eeb205e16dfd6f3e3c48d2e932eea10f046395aa20fbc5601823</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Bacteriology</topic><topic>Biochemistry, Molecular Biology</topic><topic>Life Sciences</topic><topic>Microbiology and Parasitology</topic><topic>Molecular biology</topic><topic>NlpC/P60</topic><topic>peptidoglycan hydrolase</topic><topic>α‐2‐macroglobulin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zouhir, Samira</creatorcontrib><creatorcontrib>Contreras‐Martel, Carlos</creatorcontrib><creatorcontrib>Maragno Trindade, Daniel</creatorcontrib><creatorcontrib>Attrée, Ina</creatorcontrib><creatorcontrib>Dessen, Andréa</creatorcontrib><creatorcontrib>Macheboeuf, Pauline</creatorcontrib><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zouhir, Samira</au><au>Contreras‐Martel, Carlos</au><au>Maragno Trindade, Daniel</au><au>Attrée, Ina</au><au>Dessen, Andréa</au><au>Macheboeuf, Pauline</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>MagC is a NplC/P60‐like member of the α‐2‐macroglobulin Mag complex of Pseudomonas aeruginosa that interacts with peptidoglycan</atitle><jtitle>FEBS letters</jtitle><date>2021-08</date><risdate>2021</risdate><volume>595</volume><issue>15</issue><spage>2034</spage><epage>2046</epage><pages>2034-2046</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Bacterial α‐2 macroglobulins (A2Ms) structurally resemble the large spectrum protease inhibitors of the eukaryotic immune system. 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| fulltext | fulltext |
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| ispartof | FEBS letters, 2021-08, Vol.595 (15), p.2034-2046 |
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| source | Wiley-Blackwell Journals; Wiley Free Archive; Alma/SFX Local Collection; EZB Electronic Journals Library |
| subjects | Bacteriology Biochemistry, Molecular Biology Life Sciences Microbiology and Parasitology Molecular biology NlpC/P60 peptidoglycan hydrolase α‐2‐macroglobulin |
| title | MagC is a NplC/P60‐like member of the α‐2‐macroglobulin Mag complex of Pseudomonas aeruginosa that interacts with peptidoglycan |
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