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==NMR Structure of the J-Domain and Clathrin Substrate Binding Domain of Bovine Auxilin==
==NMR Structure of the J-Domain and Clathrin Substrate Binding Domain of Bovine Auxilin==
<StructureSection load='1n4c' size='340' side='right'caption='[[1n4c]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='1n4c' size='340' side='right'caption='[[1n4c]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1n4c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovin Bovin]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N4C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N4C FirstGlance]. <br>
<table><tr><td colspan='2'>[[1n4c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N4C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N4C FirstGlance]. <br>
</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=1n4c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n4c OCA], [https://pdbe.org/1n4c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n4c RCSB], [https://www.ebi.ac.uk/pdbsum/1n4c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n4c ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1n4c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n4c OCA], [https://pdbe.org/1n4c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n4c RCSB], [https://www.ebi.ac.uk/pdbsum/1n4c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n4c ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/AUXI_BOVIN AUXI_BOVIN]] Recruits HSPA8/HSC70 to clathrin-coated vesicles and promotes uncoating of clathrin-coated vesicles.<ref>PMID:15502813</ref>
[https://www.uniprot.org/uniprot/AUXI_BOVIN AUXI_BOVIN] Recruits HSPA8/HSC70 to clathrin-coated vesicles and promotes uncoating of clathrin-coated vesicles.<ref>PMID:15502813</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1n4c ConSurf].
</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=1n4c ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The three-dimensional structure of the C-terminal 20 kDa portion of auxilin, which consists of the clathrin binding region and the C-terminal J-domain, has been determined by NMR. Auxilin is an Hsp40 family protein that catalytically supports the uncoating of clathrin-coated vesicles through recruitment of Hsc70 in an ATP hydrolysis-driven process. This 20 kDa auxilin construct contains the minimal sequential region required to uncoat clathrin-coated vesicles catalytically. The tertiary structure consists of six helices, where the first three are unique to auxilin and believed to be important in the catalytic uncoating of clathrin. The last three helices correspond to the canonical J-domain of Hsp40 proteins. The first helix, helix 1, which contains a conserved FEDLL motif believed to be necessary for clathrin binding, is transient and not packed against the rest of the structure. Helix 1 is joined to helix 2 by a flexible linker. Helix 2 packs loosely against the J-domain surface, whereas helix 3 packs tightly and makes critical contributions to the J-domain core. A long insert loop, also unique to the auxilin J-domain, is seen between helix 4 and helix 5. Comparison with a previously reported structure of auxilin containing only helices 3-6 shows a significant difference in the invariant HPD segment of the J-domain. The region where helix 1 is located corresponds to the expected region of the unstructured G/F-rich domain seen in DnaJ, i.e., the canonical N-terminal J-domain protein. In contrast, the location of helix 1 differs from the substrate binding regions of two other Hsp40 proteins, Escherichia coli Hsc20 and viral large T antigen. The variety of biological functions performed by Hsp40 proteins such as auxilin, as well as the observed differences in the structure and function of their substrate binding regions, supports the notion that Hsp40 proteins act as target-specific adaptors that recruit their more general Hsp70 partners to specific biological roles.
Structure of the functional fragment of auxilin required for catalytic uncoating of clathrin-coated vesicles.,Gruschus JM, Han CJ, Greener T, Ferretti JA, Greene LE, Eisenberg E Biochemistry. 2004 Mar 23;43(11):3111-9. PMID:15023062<ref>PMID:15023062</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1n4c" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bovin]]
[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Eisenberg, E]]
[[Category: Eisenberg E]]
[[Category: Ferretti, J A]]
[[Category: Ferretti JA]]
[[Category: Greene, L E]]
[[Category: Greene LE]]
[[Category: Greener, T]]
[[Category: Greener T]]
[[Category: Gruschus, J M]]
[[Category: Gruschus JM]]
[[Category: Han, C J]]
[[Category: Han CJ]]
[[Category: Four helix bundle]]
[[Category: Protein binding]]

Revision as of 11:45, 10 April 2024

NMR Structure of the J-Domain and Clathrin Substrate Binding Domain of Bovine AuxilinNMR Structure of the J-Domain and Clathrin Substrate Binding Domain of Bovine Auxilin

Structural highlights

1n4c is a 1 chain structure with sequence from Bos taurus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AUXI_BOVIN Recruits HSPA8/HSC70 to clathrin-coated vesicles and promotes uncoating of clathrin-coated vesicles.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Fotin A, Cheng Y, Grigorieff N, Walz T, Harrison SC, Kirchhausen T. Structure of an auxilin-bound clathrin coat and its implications for the mechanism of uncoating. Nature. 2004 Dec 2;432(7017):649-53. Epub 2004 Oct 24. PMID:15502813 doi:10.1038/nature03078
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