This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1epu

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:04, 20 March 2024) (edit) (undo)
 
(14 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1epu.jpg|left|200px]]<br /><applet load="1epu" size="350" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1epu, resolution 2.4&Aring;" />
 
-
'''X-RAY CRYSTAL STRUCTURE OF NEURONAL SEC1 FROM SQUID'''<br />
 
-
==Overview==
+
==X-RAY crystal structure of neuronal SEC1 from squid==
-
BACKGROUND: Sec1-like molecules have been implicated in a variety of eukaryotic vesicle transport processes including neurotransmitter release by exocytosis. They regulate vesicle transport by binding to a t-SNARE from the syntaxin family. This process is thought to prevent SNARE complex formation, a protein complex required for membrane fusion. Whereas Sec1 molecules are essential for neurotransmitter release and other secretory events, their interaction with syntaxin molecules seems to represent a negative regulatory step in secretion. RESULTS: Here we report the X-ray crystal structure of a neuronal Sec1 homologue from squid, s-Sec1, at 2.4 A resolution. Neuronal s-Sec1 is a modular protein that folds into a V-shaped three-domain assembly. Peptide and mutagenesis studies are discussed with respect to the mechanism of Sec1 regulation. Comparison of the structure of squid s-Sec1 with the previously determined structure of rat neuronal Sec1 (n-Sec1) bound to syntaxin-1a indicates conformational rearrangements in domain III induced by syntaxin binding. CONCLUSIONS: The crystal structure of s-Sec1 provides the molecular scaffold for a number of molecular interactions that have been reported to affect Sec1 function. The structural differences observed between s-Sec1 and the structure of a rat n-Sec1-syntaxin-1a complex suggest that local conformational changes are sufficient to release syntaxin-1a from neuronal Sec1, an active process that is thought to involve additional effector molecule(s).
+
<StructureSection load='1epu' size='340' side='right'caption='[[1epu]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
-
 
+
== Structural highlights ==
-
==About this Structure==
+
<table><tr><td colspan='2'>[[1epu]] is a 1 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=1EPU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EPU FirstGlance]. <br>
-
1EPU 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1EPU 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]] 2.4&#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>
-
==Reference==
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1epu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1epu OCA], [https://pdbe.org/1epu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1epu RCSB], [https://www.ebi.ac.uk/pdbsum/1epu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1epu ProSAT]</span></td></tr>
-
The X-ray crystal structure of neuronal Sec1 from squid sheds new light on the role of this protein in exocytosis., Bracher A, Perrakis A, Dresbach T, Betz H, Weissenhorn W, Structure. 2000 Jul 15;8(7):685-94. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10903948 10903948]
+
</table>
-
[[Category: Loligo plei]]
+
== Function ==
-
[[Category: Single protein]]
+
[https://www.uniprot.org/uniprot/O62547_DORPE O62547_DORPE]
-
[[Category: Betz, H.]]
+
== Evolutionary Conservation ==
-
[[Category: Bracher, A.]]
+
[[Image:Consurf_key_small.gif|200px|right]]
-
[[Category: Dresbach, T.]]
+
Check<jmol>
-
[[Category: Perrakis, A.]]
+
<jmolCheckbox>
-
[[Category: Weissenhorn, W.]]
+
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ep/1epu_consurf.spt"</scriptWhenChecked>
-
[[Category: helical bundle]]
+
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
-
[[Category: left-hand turn connection]]
+
<text>to colour the structure by Evolutionary Conservation</text>
-
[[Category: parallel beta-sheets]]
+
</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=1epu ConSurf].
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:30:16 2008''
+
<div style="clear:both"></div>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Doryteuthis pealeii]]
 +
[[Category: Large Structures]]
 +
[[Category: Betz H]]
 +
[[Category: Bracher A]]
 +
[[Category: Dresbach T]]
 +
[[Category: Perrakis A]]
 +
[[Category: Weissenhorn W]]

Current revision

X-RAY crystal structure of neuronal SEC1 from squid

PDB ID 1epu

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/1epu"
Personal tools