1elk

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /> <applet load="1elk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1elk, resolution 1.5&Aring;" /> '''VHS domain of TOM1 p...)
Current revision (07:04, 7 February 2024) (edit) (undo)
 
(16 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1elk.gif|left|200px]]<br />
 
-
<applet load="1elk" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1elk, resolution 1.5&Aring;" />
 
-
'''VHS domain of TOM1 protein from H. sapiens'''<br />
 
-
==Overview==
+
==VHS domain of TOM1 protein from H. sapiens==
-
VHS domains are found at the N-termini of select proteins involved in, intracellular membrane trafficking. We have determined the crystal, structure of the VHS domain of the human Tom1 (target of myb 1) protein to, 1.5 A resolution. The domain consists of eight helices arranged in a, superhelix. The surface of the domain has two main features: (1) a basic, patch on one side due to several conserved positively charged residues on, helix 3 and (2) a negatively charged ridge on the opposite side, formed by, residues on helix 2. We compare our structure to the recently obtained, structure of tandem VHS-FYVE domains from Hrs [Mao, Y., Nickitenko, A., Duan, X., Lloyd, T. E., Wu, M. N., Bellen, H., and Quiocho, F. A. (2000), Cell 100, 447-456]. Key features of the interaction surface between the, FYVE and VHS domains of Hrs, involving helices 2 and 4 of the VHS domain, are conserved in the VHS domain of Tom1, even though Tom1 does not have a, FYVE domain. We also compare the structures of the VHS domains of Tom1 and, Hrs to the recently obtained structure of the ENTH domain of epsin-1, [Hyman, J., Chen, H., Di Fiore, P. P., De Camilli, P., and Brunger, A. T., (2000) J. Cell Biol. 149, 537-546]. Comparison of the two VHS domains and, the ENTH domain reveals a conserved surface, composed of helices 2 and 4, that is utilized for protein-protein interactions. In addition, VHS, domain-containing proteins are often localized to membranes. We suggest, that the conserved positively charged surface of helix 3 in VHS and ENTH, domains plays a role in membrane binding.
+
<StructureSection load='1elk' size='340' side='right'caption='[[1elk]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
-
 
+
== Structural highlights ==
-
==About this Structure==
+
<table><tr><td colspan='2'>[[1elk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ELK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ELK FirstGlance]. <br>
-
1ELK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ELK OCA].
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</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=1elk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1elk OCA], [https://pdbe.org/1elk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1elk RCSB], [https://www.ebi.ac.uk/pdbsum/1elk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1elk ProSAT]</span></td></tr>
-
==Reference==
+
</table>
-
Structure of the VHS domain of human Tom1 (target of myb 1): insights into interactions with proteins and membranes., Misra S, Beach BM, Hurley JH, Biochemistry. 2000 Sep 19;39(37):11282-90. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10985773 10985773]
+
== Function ==
 +
[https://www.uniprot.org/uniprot/TOM1_HUMAN TOM1_HUMAN] May be involved in intracellular trafficking. Probable association with membranes.
 +
== 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/el/1elk_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=1elk ConSurf].
 +
<div style="clear:both"></div>
 +
__TOC__
 +
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Beach, B.]]
+
[[Category: Beach B]]
-
[[Category: Hurley, J.H.]]
+
[[Category: Hurley JH]]
-
[[Category: Misra, S.]]
+
[[Category: Misra S]]
-
[[Category: superhelix of helices]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:44:36 2007''
+

Current revision

VHS domain of TOM1 protein from H. sapiens

PDB ID 1elk

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/1elk"
Personal tools