1w9a

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1w9a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1w9a, resolution 1.80&Aring;" /> '''CRYSTAL STRUCTURE OF...)
Current revision (07:41, 23 October 2024) (edit) (undo)
 
(17 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1w9a.gif|left|200px]]<br /><applet load="1w9a" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1w9a, resolution 1.80&Aring;" />
 
-
'''CRYSTAL STRUCTURE OF RV1155 FROM MYCOBACTERIUM TUBERCULOSIS'''<br />
 
-
==Overview==
+
==Crystal structure of Rv1155 from Mycobacterium tuberculosis==
-
With the aim of elucidating the biological function of hypothetical, proteins unique amongst the Actynomyces sub-group of bacteria, we have, solved the crystal structure of the conserved hypothetical protein Rv1155, from Mycobacterium tuberculosis at 1.8 A resolution. Rv1155 is a homodimer, both in the crystal structure and in solution and folds into two separate, domains consisting of a six-stranded anti-parallel beta-barrel fold, flanked by two alpha-helices and a helix-turn-helix domain. Both domains, contribute to the formation of two deep clefts at the dimer interface. The, overall fold of Rv1155 strikingly resembles that of flavin, mononucleotide-binding protein and pyridoxamine 5'-phosphate oxydase, but, the architecture of the putative binding pocket is markedly different, consistent with the lack of color of Rv1155 and its inability to bind FMN., Rv1155 thus appears to belong to a group of proteins with stringent, conservation of the binding cleft, having evolved towards a new binding, function.
+
<StructureSection load='1w9a' size='340' side='right'caption='[[1w9a]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1w9a]] is a 2 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=1W9A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W9A FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=1w9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w9a OCA], [https://pdbe.org/1w9a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w9a RCSB], [https://www.ebi.ac.uk/pdbsum/1w9a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w9a ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/F420R_MYCTU F420R_MYCTU] F420H(2)-dependent reductase able to catalyze the reduction of biliverdin-IXalpha to bilirubin-IXalpha in vitro. However, kinetic parameters show that it is less efficient than the biliverdin reductase Rv2074 and suggest biliverdin-IXalpha is unlikely to be the native substrate of Rv1155, which probably catalyzes the reduction of an alternative molecule in vivo (PubMed:27364382). Binds coenzyme F420, but does not bind FMN or other flavins (PubMed:25644473). Cannot use pyridoxine 5'-phosphate, pyridoxamine 5'-phosphate, pyridoxal 5'-phosphate (PLP), the anti-tuberculosis drug PA-824 or aflatoxin analogs as substrates (PubMed:25644473).<ref>PMID:25644473</ref> <ref>PMID:27364382</ref>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w9/1w9a_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</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=1w9a ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
With the aim of elucidating the biological function of hypothetical proteins unique amongst the Actynomyces sub-group of bacteria, we have solved the crystal structure of the conserved hypothetical protein Rv1155 from Mycobacterium tuberculosis at 1.8 A resolution. Rv1155 is a homodimer both in the crystal structure and in solution and folds into two separate domains consisting of a six-stranded anti-parallel beta-barrel fold flanked by two alpha-helices and a helix-turn-helix domain. Both domains contribute to the formation of two deep clefts at the dimer interface. The overall fold of Rv1155 strikingly resembles that of flavin mononucleotide-binding protein and pyridoxamine 5'-phosphate oxydase, but the architecture of the putative binding pocket is markedly different, consistent with the lack of color of Rv1155 and its inability to bind FMN. Rv1155 thus appears to belong to a group of proteins with stringent conservation of the binding cleft, having evolved towards a new binding function.
-
==About this Structure==
+
Crystal structure of the conserved hypothetical protein Rv1155 from Mycobacterium tuberculosis.,Canaan S, Sulzenbacher G, Roig-Zamboni V, Scappuccini-Calvo L, Frassinetti F, Maurin D, Cambillau C, Bourne Y FEBS Lett. 2005 Jan 3;579(1):215-21. PMID:15620716<ref>PMID:15620716</ref>
-
1W9A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W9A OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
Crystal structure of the conserved hypothetical protein Rv1155 from Mycobacterium tuberculosis., Canaan S, Sulzenbacher G, Roig-Zamboni V, Scappuccini-Calvo L, Frassinetti F, Maurin D, Cambillau C, Bourne Y, FEBS Lett. 2005 Jan 3;579(1):215-21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15620716 15620716]
+
</div>
-
[[Category: Mycobacterium tuberculosis]]
+
<div class="pdbe-citations 1w9a" style="background-color:#fffaf0;"></div>
-
[[Category: Single protein]]
+
== References ==
-
[[Category: Bourne, Y.]]
+
<references/>
-
[[Category: Cambillau, C.]]
+
__TOC__
-
[[Category: Canaan, S.]]
+
</StructureSection>
-
[[Category: Frassinetti-Calvo, F.]]
+
[[Category: Large Structures]]
-
[[Category: Maurin, D.]]
+
[[Category: Mycobacterium tuberculosis H37Rv]]
-
[[Category: Roig-Zamboni, V.]]
+
[[Category: Bourne Y]]
-
[[Category: Scappuccini, L.]]
+
[[Category: Cambillau C]]
-
[[Category: Sulzenbacher, G.]]
+
[[Category: Cannan S]]
-
[[Category: hypothetical protein]]
+
[[Category: Frassinetti F]]
-
[[Category: mycobacterium tuberculosis]]
+
[[Category: Maurien D]]
-
[[Category: related to fmn-binding proteins]]
+
[[Category: Roig-Zamboni V]]
-
[[Category: structural genomics]]
+
[[Category: Scappuccini L]]
-
 
+
[[Category: Sulzenbacher G]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:35:19 2007''
+

Current revision

Crystal structure of Rv1155 from Mycobacterium tuberculosis

PDB ID 1w9a

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools