1fvf

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1fvf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fvf, resolution 3.2&Aring;" /> '''CRYSTAL STRUCTURE ANA...)
Current revision (06:05, 9 August 2023) (edit) (undo)
 
(16 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1fvf.gif|left|200px]]<br /><applet load="1fvf" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1fvf, resolution 3.2&Aring;" />
 
-
'''CRYSTAL STRUCTURE ANALYSIS OF NEURONAL SEC1 FROM THE SQUID L. PEALEI'''<br />
 
-
==Overview==
+
==CRYSTAL STRUCTURE ANALYSIS OF NEURONAL SEC1 FROM THE SQUID L. PEALEI==
-
Sec1 molecules associate with t-SNAREs from the syntaxin family in a, heterodimeric complex that plays an essential role in vesicle transport, and membrane fusion. Neuronal rat n-Sec1 has an arch-shaped three-domain, structure, which binds syntaxin 1a through contacts in domains 1 and 3. In, both rat nSec1 and homologous squid s-Sec1, a potential effector-molecule, binding-pocket is shaped by residues from domains 1 and 2 and is localized, on the opposite side of the syntaxin 1a interaction site. Comparison of, several crystal forms of unliganded neuronal squid Sec1 indicates a hinge, region between domains 1 and 2 which allows domain 1 to rotate along a, central axis. This movement could release syntaxin 1a upon interaction, with a yet unspecified Sec1 effector molecule(s). The binding of an, effector protein may also directly affect the conformation of the helical, hairpin of domain 3, which contributes the other significant syntaxin 1a, binding sites in the rat nSec1/syntaxin 1a complex structure but adopts, multiple conformations in the unliganded s-Sec1 structures reported here.
+
<StructureSection load='1fvf' size='340' side='right'caption='[[1fvf]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1fvf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Doryteuthis_pealeii Doryteuthis pealeii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FVF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FVF 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]] 3.2&#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=1fvf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fvf OCA], [https://pdbe.org/1fvf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fvf RCSB], [https://www.ebi.ac.uk/pdbsum/1fvf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fvf ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/O62547_DORPE O62547_DORPE]
 +
== 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/fv/1fvf_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=1fvf ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Sec1 molecules associate with t-SNAREs from the syntaxin family in a heterodimeric complex that plays an essential role in vesicle transport and membrane fusion. Neuronal rat n-Sec1 has an arch-shaped three-domain structure, which binds syntaxin 1a through contacts in domains 1 and 3. In both rat nSec1 and homologous squid s-Sec1, a potential effector-molecule binding-pocket is shaped by residues from domains 1 and 2 and is localized on the opposite side of the syntaxin 1a interaction site. Comparison of several crystal forms of unliganded neuronal squid Sec1 indicates a hinge region between domains 1 and 2 which allows domain 1 to rotate along a central axis. This movement could release syntaxin 1a upon interaction with a yet unspecified Sec1 effector molecule(s). The binding of an effector protein may also directly affect the conformation of the helical hairpin of domain 3, which contributes the other significant syntaxin 1a binding sites in the rat nSec1/syntaxin 1a complex structure but adopts multiple conformations in the unliganded s-Sec1 structures reported here.
-
==About this Structure==
+
Crystal structures of neuronal squid Sec1 implicate inter-domain hinge movement in the release of t-SNAREs.,Bracher A, Weissenhorn W J Mol Biol. 2001 Feb 9;306(1):7-13. PMID:11178889<ref>PMID:11178889</ref>
-
1FVF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Loligo_plei Loligo plei]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FVF OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
Crystal structures of neuronal squid Sec1 implicate inter-domain hinge movement in the release of t-SNAREs., Bracher A, Weissenhorn W, J Mol Biol. 2001 Feb 9;306(1):7-13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11178889 11178889]
+
</div>
-
[[Category: Loligo plei]]
+
<div class="pdbe-citations 1fvf" style="background-color:#fffaf0;"></div>
-
[[Category: Single protein]]
+
== References ==
-
[[Category: Bracher, A.]]
+
<references/>
-
[[Category: Weissenhorn, W.]]
+
__TOC__
-
[[Category: dimer]]
+
</StructureSection>
-
[[Category: helical bundle]]
+
[[Category: Doryteuthis pealeii]]
-
[[Category: left-hand turn connection]]
+
[[Category: Large Structures]]
-
[[Category: parallel beta-sheets]]
+
[[Category: Bracher A]]
-
 
+
[[Category: Weissenhorn W]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 00:24:56 2007''
+

Current revision

CRYSTAL STRUCTURE ANALYSIS OF NEURONAL SEC1 FROM THE SQUID L. PEALEI

PDB ID 1fvf

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/1fvf"
Personal tools