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.


5has

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (12:31, 6 March 2024) (edit) (undo)
 
(One intermediate revision not shown.)
Line 3: Line 3:
<StructureSection load='5has' size='340' side='right'caption='[[5has]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
<StructureSection load='5has' size='340' side='right'caption='[[5has]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5has]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HAS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HAS FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5has]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermothielavioides_terrestris Thermothielavioides terrestris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HAS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HAS FirstGlance]. <br>
-
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5has FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5has OCA], [http://pdbe.org/5has PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5has RCSB], [http://www.ebi.ac.uk/pdbsum/5has PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5has ProSAT]</span></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.653&#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=5has FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5has OCA], [https://pdbe.org/5has PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5has RCSB], [https://www.ebi.ac.uk/pdbsum/5has PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5has ProSAT]</span></td></tr>
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/A0A140UHP8_9PEZI A0A140UHP8_9PEZI]
-
The Golgi complex is the central sorting compartment of eukaryotic cells. Arf guanine nucleotide exchange factors (Arf-GEFs) regulate virtually all traffic through the Golgi by activating Arf GTPase trafficking pathways. The Golgi Arf-GEFs contain multiple autoregulatory domains, but the precise mechanisms underlying their function remain largely undefined. We report a crystal structure revealing that the N-terminal DCB and HUS regulatory domains of the Arf-GEF Sec7 form a single structural unit. We demonstrate that the established role of the N-terminal region in dimerization is not conserved; instead, a C-terminal autoinhibitory domain is responsible for dimerization of Sec7. We find that the DCB/HUS domain amplifies the ability of Sec7 to activate Arf1 on the membrane surface by facilitating membrane insertion of the Arf1 amphipathic helix. This enhancing function of the Sec7 N-terminal domains is consistent with the high rate of Arf1-dependent trafficking to the plasma membrane necessary for maximal cell growth.
+
-
 
+
-
The Sec7 N-terminal regulatory domains facilitate membrane-proximal activation of the Arf1 GTPase.,Richardson BC, Halaby SL, Gustafson MA, Fromme JC Elife. 2016 Jan 14;5. pii: e12411. doi: 10.7554/eLife.12411. PMID:26765562<ref>PMID:26765562</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 5has" style="background-color:#fffaf0;"></div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Fromme, J C]]
+
[[Category: Thermothielavioides terrestris]]
-
[[Category: Richardson, B C]]
+
[[Category: Fromme JC]]
-
[[Category: Arf-gef]]
+
[[Category: Richardson BC]]
-
[[Category: Armadillo]]
+
-
[[Category: Protein transport]]
+
-
[[Category: Tgn]]
+
-
[[Category: Transport]]
+

Current revision

Crystal structure of the N-terminal DCB-HUS domain of T. terrestris Sec7

PDB ID 5has

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/5has"
Personal tools