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[[Image:4hl4.jpg|left|200px]]


{{STRUCTURE_4hl4| PDB=4hl4 | SCENE= }}
==Crystal structure of the human TBC1D20 RabGAP domain==
<StructureSection load='4hl4' size='340' side='right' caption='[[4hl4]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4hl4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HL4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HL4 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4hlq|4hlq]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TBC1D20, C20orf140 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4hl4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hl4 OCA], [http://pdbe.org/4hl4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hl4 RCSB], [http://www.ebi.ac.uk/pdbsum/4hl4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hl4 ProSAT]</span></td></tr>
</table>
== Disease ==
[[http://www.uniprot.org/uniprot/TBC20_HUMAN TBC20_HUMAN]] Micro syndrome. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
[[http://www.uniprot.org/uniprot/TBC20_HUMAN TBC20_HUMAN]] GTPase-activating protein specific for Rab1 and Rab2 small GTPase families for which it can accelerate the intrinsic GTP hydrolysis rate by more than five orders of magnitude.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Rab GTPases, key regulators of vesicular transport, hydrolyze GTP very slowly unless assisted by Rab GTPase-activating proteins (RabGAPs). Dysfunction of RabGAPs is involved in many diseases. By combining X-ray structure analysis and time-resolved FTIR spectroscopy we reveal here the detailed molecular reaction mechanism of a complex between human Rab and RabGAP at the highest possible spatiotemporal resolution and in atomic detail. A glutamine residue of Rab proteins (cis-glutamine) that is essential for intrinsic activity is less important in the GAP-activated reaction. During generation of the RabGAP.Rab:GTP complex, there is a rapid conformational change in which the cis-glutamine is replaced by a glutamine from RabGAP (trans-glutamine); this differs from the RasGAP mechanism, where the cis-glutamine is also important for GAP catalysis. However, as in the case of Ras, a trans-arginine is also recruited to complete the active center during this conformational change. In contrast to the RasGAP mechanism, an accumulation of a state in which phosphate is bound is not observed, and bond breakage is the rate-limiting step. The movement of trans-glutamine and trans-arginine into the catalytic site and bond breakage during hydrolysis are monitored in real time. The combination of X-ray structure analysis and time-resolved FTIR spectroscopy provides detailed insight in the catalysis of human Rab GTPases.


===Crystal structure of the human TBC1D20 RabGAP domain===
Catalytic mechanism of a mammalian Rab{middle dot}RabGAP complex in atomic detail.,Gavriljuk K, Gazdag EM, Itzen A, Kotting C, Goody RS, Gerwert K Proc Natl Acad Sci U S A. 2012 Dec 26;109(52):21348-53. doi:, 10.1073/pnas.1214431110. Epub 2012 Dec 12. PMID:23236136<ref>PMID:23236136</ref>


{{ABSTRACT_PUBMED_23236136}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 4hl4" style="background-color:#fffaf0;"></div>
[[4hl4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HL4 OCA].
== References ==
[[Category: Homo sapiens]]
<references/>
[[Category: Gavriljuk, K.]]
__TOC__
[[Category: Gazdag, E M.]]
</StructureSection>
[[Category: Gerwert, K.]]
[[Category: Human]]
[[Category: Goody, R S.]]
[[Category: Gavriljuk, K]]
[[Category: Itzen, A.]]
[[Category: Gazdag, E M]]
[[Category: Koetting, C.]]
[[Category: Gerwert, K]]
[[Category: Goody, R S]]
[[Category: Itzen, A]]
[[Category: Koetting, C]]
[[Category: Catalytic domain]]
[[Category: Catalytic domain]]
[[Category: Fluoride]]
[[Category: Fluoride]]
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