Structure predictions and surface charge of nitrogenase flavodoxins from Klebsiella pneumoniae and Azotobacter vinelandii
A first approximation to the tertiary structure of the nitrogenase flavodoxins of Klebsiella pneumoniae and Azotobacter vinelandii can be obtained by superimposing their amino acid sequences upon the crystallographically determined structure of the long‐chain flavodoxin from Anacystis nidulans. This...
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| Veröffentlicht in: | European journal of biochemistry 1986-09, Vol.159 (3), p.549-553 |
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| container_title | European journal of biochemistry |
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| creator | Drummond, M.H |
| description | A first approximation to the tertiary structure of the nitrogenase flavodoxins of Klebsiella pneumoniae and Azotobacter vinelandii can be obtained by superimposing their amino acid sequences upon the crystallographically determined structure of the long‐chain flavodoxin from Anacystis nidulans. This procedure is validated by secondary structure predictions based on the sequence alone and by the distribution of polar and hydrophobic residues. It reveals, among other things, a distinctive distribution of surface charge peculiar to the nitrogenase flavodoxins, which is probably important in determining the kinetics of electron transfer with their physiological redox partners. The most likely positions of the phosphodiester bridge which has been described in the A. vinelandii molecule can also be assessed. |
| doi_str_mv | 10.1111/j.1432-1033.1986.tb09921.x |
| format | Article |
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This procedure is validated by secondary structure predictions based on the sequence alone and by the distribution of polar and hydrophobic residues. It reveals, among other things, a distinctive distribution of surface charge peculiar to the nitrogenase flavodoxins, which is probably important in determining the kinetics of electron transfer with their physiological redox partners. 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This procedure is validated by secondary structure predictions based on the sequence alone and by the distribution of polar and hydrophobic residues. It reveals, among other things, a distinctive distribution of surface charge peculiar to the nitrogenase flavodoxins, which is probably important in determining the kinetics of electron transfer with their physiological redox partners. The most likely positions of the phosphodiester bridge which has been described in the A. vinelandii molecule can also be assessed.</description><subject>Amino Acid Sequence</subject><subject>amino acids</subject><subject>Applied sciences</subject><subject>Azotobacter - enzymology</subject><subject>Azotobacter vinelandii</subject><subject>Electrochemistry</subject><subject>Exact sciences and technology</subject><subject>Flavodoxin - genetics</subject><subject>Flavoproteins - genetics</subject><subject>Klebsiella pneumoniae</subject><subject>Klebsiella pneumoniae - enzymology</subject><subject>Models, Molecular</subject><subject>nitrogenase</subject><subject>Nitrogenase - metabolism</subject><subject>Other techniques and industries</subject><subject>Oxidation-Reduction</subject><subject>Phosphates - analysis</subject><subject>Protein Conformation</subject><subject>sequences</subject><subject>Surface Properties</subject><subject>Synechococcus</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1986</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVklGP1CAUhYnRrOPqTzASY3xrhUJh8GWzbnbVuIkP4z6TWwojk7aM0K4z_nqp08y7vEDuOffcmy8g9JaSkubzYVdSzqqCEsZKqtaiHBuiVEXLwxO0OktP0YoQyotK1eI5epHSjhAilJAX6ILVjEhBVui4GeNkxilavI-29Wb0YUgYhhanKTowFpufELcWB4cHP8awtQMki10Hj6ENB5_dLoYef-tsk7ztOsD7wU59GDzYf0HXf8IYGjCjjfjRD7bLRe9fomcOumRfLfcleri7_XHzpbj__vnrzfV9YbisVaEYbVpCK2dMJSm3FEh-1rZqhYGqroVsiIBGOu4UAWDKNFIy1wrhJJeNYJfo_Sl3H8OvyaZR9z6Zec_BhilpKQmvOKfZ-PFkNDGkFK3T--h7iEdNiZ65652e4eoZrp6564W7PuTm18uUqelte25dQGf93aJDMtC5CIPx6WxbM76uBcu2q5Ptt-_s8T8W0He3nzY1VznhzSnBQdCwjXnIw6YilOWvIGrFOfsL31WsHg</recordid><startdate>19860915</startdate><enddate>19860915</enddate><creator>Drummond, M.H</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</general><scope>FBQ</scope><scope>IQODW</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></search><sort><creationdate>19860915</creationdate><title>Structure predictions and surface charge of nitrogenase flavodoxins from Klebsiella pneumoniae and Azotobacter vinelandii</title><author>Drummond, M.H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4759-931bd012fcc2714e1a0fcc5e2d6ca25567b06ab7f4f90aa39cb773fd66f747b63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1986</creationdate><topic>Amino Acid Sequence</topic><topic>amino acids</topic><topic>Applied sciences</topic><topic>Azotobacter - enzymology</topic><topic>Azotobacter vinelandii</topic><topic>Electrochemistry</topic><topic>Exact sciences and technology</topic><topic>Flavodoxin - genetics</topic><topic>Flavoproteins - genetics</topic><topic>Klebsiella pneumoniae</topic><topic>Klebsiella pneumoniae - enzymology</topic><topic>Models, Molecular</topic><topic>nitrogenase</topic><topic>Nitrogenase - metabolism</topic><topic>Other techniques and industries</topic><topic>Oxidation-Reduction</topic><topic>Phosphates - analysis</topic><topic>Protein Conformation</topic><topic>sequences</topic><topic>Surface Properties</topic><topic>Synechococcus</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Drummond, M.H</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</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><jtitle>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Drummond, M.H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structure predictions and surface charge of nitrogenase flavodoxins from Klebsiella pneumoniae and Azotobacter vinelandii</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1986-09-15</date><risdate>1986</risdate><volume>159</volume><issue>3</issue><spage>549</spage><epage>553</epage><pages>549-553</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><coden>EJBCAI</coden><abstract>A first approximation to the tertiary structure of the nitrogenase flavodoxins of Klebsiella pneumoniae and Azotobacter vinelandii can be obtained by superimposing their amino acid sequences upon the crystallographically determined structure of the long‐chain flavodoxin from Anacystis nidulans. This procedure is validated by secondary structure predictions based on the sequence alone and by the distribution of polar and hydrophobic residues. It reveals, among other things, a distinctive distribution of surface charge peculiar to the nitrogenase flavodoxins, which is probably important in determining the kinetics of electron transfer with their physiological redox partners. The most likely positions of the phosphodiester bridge which has been described in the A. vinelandii molecule can also be assessed.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>3530760</pmid><doi>10.1111/j.1432-1033.1986.tb09921.x</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-2956 |
| ispartof | European journal of biochemistry, 1986-09, Vol.159 (3), p.549-553 |
| issn | 0014-2956 1432-1033 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_77042441 |
| source | MEDLINE; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence amino acids Applied sciences Azotobacter - enzymology Azotobacter vinelandii Electrochemistry Exact sciences and technology Flavodoxin - genetics Flavoproteins - genetics Klebsiella pneumoniae Klebsiella pneumoniae - enzymology Models, Molecular nitrogenase Nitrogenase - metabolism Other techniques and industries Oxidation-Reduction Phosphates - analysis Protein Conformation sequences Surface Properties Synechococcus |
| title | Structure predictions and surface charge of nitrogenase flavodoxins from Klebsiella pneumoniae and Azotobacter vinelandii |
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