1rfe: Difference between revisions
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==Crystal structure of conserved hypothetical protein Rv2991 from Mycobacterium tuberculosis== | ==Crystal structure of conserved hypothetical protein Rv2991 from Mycobacterium tuberculosis== | ||
<StructureSection load='1rfe' size='340' side='right' caption='[[1rfe]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1rfe' size='340' side='right'caption='[[1rfe]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1rfe]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RFE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RFE FirstGlance]. <br> | <table><tr><td colspan='2'>[[1rfe]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RFE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RFE FirstGlance]. <br> | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1rfe ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1rfe ConSurf]. | ||
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== Publication Abstract from PubMed == | |||
The crystal structure of the conserved hypothetical protein Rv2991 from Mycobacterium tuberculosis has been solved by SAD using seleno-methionine substituted protein. The dimeric biological assembly and the sequence and fold conservation are typical of F420 cofactor binding enzymes. Despite Rv2991 still being of unknown function, sequence and structural comparison with similar proteins enable a role to be proposed for its C-terminal stretch of residues in recognizing and orienting the substrate. In addition, the C-terminus is involved in both protein folding and determining the size of the active site cavity. | |||
The crystal structure of Rv2991 from Mycobacterium tuberculosis: An F420 binding protein with unknown function.,Benini S, Haouz A, Proux F, Alzari P, Wilson K J Struct Biol. 2019 Mar 16. pii: S1047-8477(19)30051-6. doi:, 10.1016/j.jsb.2019.03.006. PMID:30890426<ref>PMID:30890426</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1rfe" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Myctu]] | [[Category: Myctu]] | ||
[[Category: Alzari, P]] | [[Category: Alzari, P]] | ||
Revision as of 09:15, 17 April 2019
Crystal structure of conserved hypothetical protein Rv2991 from Mycobacterium tuberculosisCrystal structure of conserved hypothetical protein Rv2991 from Mycobacterium tuberculosis
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of the conserved hypothetical protein Rv2991 from Mycobacterium tuberculosis has been solved by SAD using seleno-methionine substituted protein. The dimeric biological assembly and the sequence and fold conservation are typical of F420 cofactor binding enzymes. Despite Rv2991 still being of unknown function, sequence and structural comparison with similar proteins enable a role to be proposed for its C-terminal stretch of residues in recognizing and orienting the substrate. In addition, the C-terminus is involved in both protein folding and determining the size of the active site cavity. The crystal structure of Rv2991 from Mycobacterium tuberculosis: An F420 binding protein with unknown function.,Benini S, Haouz A, Proux F, Alzari P, Wilson K J Struct Biol. 2019 Mar 16. pii: S1047-8477(19)30051-6. doi:, 10.1016/j.jsb.2019.03.006. PMID:30890426[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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