3fz0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: '''Unreleased structure''' The entry 3fz0 is ON HOLD Authors: Vandemeulebroucke, A., Minici, C., Bruno, I., Muzzolini, L., Tornaghi, P., Parkin, D.W., Schramm, V.L., Versees, W., Steyae...)
Current revision (15:34, 1 November 2023) (edit) (undo)
 
(10 intermediate revisions not shown.)
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 3fz0 is ON HOLD
+
==Inosine-Guanosine Nucleoside Hydrolase (IG-NH)==
 +
<StructureSection load='3fz0' size='340' side='right'caption='[[3fz0]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[3fz0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_brucei Trypanosoma brucei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FZ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FZ0 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]] 2.5&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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=3fz0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fz0 OCA], [https://pdbe.org/3fz0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fz0 RCSB], [https://www.ebi.ac.uk/pdbsum/3fz0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fz0 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/Q57X73_TRYB2 Q57X73_TRYB2]
 +
== 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/fz/3fz0_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=3fz0 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Trypanosomes are purine-auxotrophic parasites that depend upon nucleoside hydrolase (NH) activity to salvage nitrogenous bases necessary for nucleic acid and cofactor synthesis. Nonspecific and purine-specific NHs have been widely studied, yet little is known about the 6-oxopurine-specific isozymes, although they are thought to play a primary role in the catabolism of exogenously derived nucleosides. Here, we report the first functional and structural characterization of the inosine-guanosine-specific NH from Trypanosoma brucei brucei. The enzyme shows near diffusion-limited efficiency coupled with a clear specificity for 6-oxopurine nucleosides achieved through a catalytic selection of these substrates. Pre-steady-state kinetic analysis reveals ordered product release, and a rate-limiting structural rearrangement that is associated with the release of the product, ribose. The crystal structure of this trypanosomal NH determined to 2.5 A resolution reveals distinctive features compared to those of both purine- and pyrimidine-specific isozymes in the framework of the conserved and versatile NH fold. Nanomolar iminoribitol-based inhibitors identified in this study represent important lead compounds for the development of novel therapeutic strategies against trypanosomal diseases.
-
Authors: Vandemeulebroucke, A., Minici, C., Bruno, I., Muzzolini, L., Tornaghi, P., Parkin, D.W., Schramm, V.L., Versees, W., Steyaert, J., Degano, M.
+
Structure and mechanism of the 6-oxopurine nucleosidase from Trypanosoma brucei brucei.,Vandemeulebroucke A, Minici C, Bruno I, Muzzolini L, Tornaghi P, Parkin DW, Versees W, Steyaert J, Degano M Biochemistry. 2010 Oct 19;49(41):8999-9010. PMID:20825170<ref>PMID:20825170</ref>
-
Description: Inosine-Guanosine Nucleoside Hydrolase (IG-NH)
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 11 12:36:02 2009''
+
<div class="pdbe-citations 3fz0" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
 +
[[Category: Trypanosoma brucei]]
 +
[[Category: Bruno I]]
 +
[[Category: Degano M]]
 +
[[Category: Minici C]]
 +
[[Category: Muzzolini L]]
 +
[[Category: Parkin DW]]
 +
[[Category: Schramm VL]]
 +
[[Category: Steyaert J]]
 +
[[Category: Tornaghi P]]
 +
[[Category: Vandemeulebroucke A]]
 +
[[Category: Versees W]]

Current revision

Inosine-Guanosine Nucleoside Hydrolase (IG-NH)

PDB ID 3fz0

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools