1rfe: Difference between revisions

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<StructureSection load='1rfe' size='340' side='right'caption='[[1rfe]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1rfe' size='340' side='right'caption='[[1rfe]], [[Resolution|resolution]] 2.00&Aring;' 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://proteopedia.org/fgij/fg.htm?mol=1RFE FirstGlance]. <br>
<table><tr><td colspan='2'>[[1rfe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1RFE FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSX:S-OXY+CYSTEINE'>CSX</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1rfe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rfe OCA], [http://pdbe.org/1rfe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rfe RCSB], [http://www.ebi.ac.uk/pdbsum/1rfe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rfe ProSAT], [http://www.topsan.org/Proteins/TBSGC/1rfe TOPSAN]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSX:S-OXY+CYSTEINE'>CSX</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rfe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rfe OCA], [https://pdbe.org/1rfe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rfe RCSB], [https://www.ebi.ac.uk/pdbsum/1rfe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rfe ProSAT], [https://www.topsan.org/Proteins/TBSGC/1rfe TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O53240_MYCTU O53240_MYCTU]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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&reg;/PubMed&reg;, 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: Large Structures]]
[[Category: Myctu]]
[[Category: Mycobacterium tuberculosis H37Rv]]
[[Category: Alzari, P]]
[[Category: Alzari P]]
[[Category: Benini, S]]
[[Category: Benini S]]
[[Category: Betton, J M]]
[[Category: Betton JM]]
[[Category: Dodson, G G]]
[[Category: Dodson GG]]
[[Category: Haouz, A]]
[[Category: Haouz A]]
[[Category: Proux, F]]
[[Category: Proux F]]
[[Category: Structural genomic]]
[[Category: Wilson KS]]
[[Category: Wilson, K S]]
[[Category: Fmn binding]]
[[Category: Mycobacterium tuberculosis]]
[[Category: PSI, Protein structure initiative]]
[[Category: Tb]]
[[Category: Tbsgc]]
[[Category: Unknown function]]

Latest revision as of 11:22, 1 May 2024

Crystal structure of conserved hypothetical protein Rv2991 from Mycobacterium tuberculosisCrystal structure of conserved hypothetical protein Rv2991 from Mycobacterium tuberculosis

Structural highlights

1rfe is a 1 chain structure with sequence from Mycobacterium tuberculosis H37Rv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

O53240_MYCTU

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1rfe, resolution 2.00Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
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