2ax5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (11:18, 22 May 2024) (edit) (undo)
 
(9 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:2ax5.png|left|200px]]
 
-
<!--
+
==Solution Structure of Urm1 from Saccharomyces Cerevisiae==
-
The line below this paragraph, containing "STRUCTURE_2ax5", creates the "Structure Box" on the page.
+
<StructureSection load='2ax5' size='340' side='right'caption='[[2ax5]]' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[2ax5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AX5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AX5 FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2ax5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ax5 OCA], [https://pdbe.org/2ax5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ax5 RCSB], [https://www.ebi.ac.uk/pdbsum/2ax5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ax5 ProSAT]</span></td></tr>
-
{{STRUCTURE_2ax5| PDB=2ax5 | SCENE= }}
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/URM1_YEAST URM1_YEAST] Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions. Serves as sulfur donor in tRNA 2-thiolation reaction by being thiocarboxylated (-COSH) at its C-terminus by UBA4. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. May also act as an ubiquitin-like protein that is covalently conjugated to other proteins such as AHP1; the relevance of such function is however unclear in vivo. Indirectly involved in oxidative stress response and regulation of budding and haploid invasive growth.<ref>PMID:10713047</ref> <ref>PMID:14555475</ref> <ref>PMID:14551258</ref> <ref>PMID:18664566</ref> <ref>PMID:18755837</ref> <ref>PMID:19145231</ref> <ref>PMID:19151091</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/ax/2ax5_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=2ax5 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Protein modifiers are involved in diverse biological processes and regulate the activity or function of target proteins by covalently conjugating to them. Although ubiquitin and a number of ubiquitin-like protein modifiers (Ubls) in eukaryotes have been identified, no protein modifier has been found in prokaryotes; thus, their evolutionary origin remains a puzzle. To infer the evolutionary relationships between the protein modifiers and sulfur carrier proteins, we solved the solution NMR structure of the Urm1 (ubiquitin-related modifier-1) protein from Saccharomyces cerevisiae. Both structural comparison and phylogenetic analysis of the ubiquitin superfamily, with emphasis on the Urm1 family, indicate that Urm1 is the unique "molecular fossil" that has the most conserved structural and sequence features of the common ancestor of the entire superfamily. The similarities of 3D structure and hydrophobic and electrostatic surface features between Urm1 and MoaD (molybdopterin synthase small subunit) suggest that they may interact with partners in a similar manner, and similarities between Urm1-Uba4 and MoaD-MoeB establish an evolutionary link between ATP-dependent protein conjugation in eukaryotes and ATP-dependent cofactor sulfuration.
-
===Solution Structure of Urm1 from Saccharomyces Cerevisae===
+
Solution structure of Urm1 and its implications for the origin of protein modifiers.,Xu J, Zhang J, Wang L, Zhou J, Huang H, Wu J, Zhong Y, Shi Y Proc Natl Acad Sci U S A. 2006 Aug 1;103(31):11625-30. Epub 2006 Jul 24. PMID:16864801<ref>PMID:16864801</ref>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
==About this Structure==
+
</div>
-
2AX5 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AX5 OCA].
+
<div class="pdbe-citations 2ax5" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
-
[[Category: Huang, H.]]
+
[[Category: Huang H]]
-
[[Category: Shi, Y.]]
+
[[Category: Shi Y]]
-
[[Category: Wu, J.]]
+
[[Category: Wu J]]
-
[[Category: Xu, J.]]
+
[[Category: Xu J]]
-
[[Category: Zhang, J.]]
+
[[Category: Zhang J]]
-
[[Category: Beta grasp fold]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 07:07:21 2009''
+

Current revision

Solution Structure of Urm1 from Saccharomyces Cerevisiae

PDB ID 2ax5

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ax5"
Personal tools