2qld: Difference between revisions

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<StructureSection load='2qld' size='340' side='right'caption='[[2qld]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='2qld' size='340' side='right'caption='[[2qld]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2qld]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QLD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QLD FirstGlance]. <br>
<table><tr><td colspan='2'>[[2qld]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QLD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QLD FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DNAJB1, DNAJ1, HDJ1, HSPF1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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]] 2.7&#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=2qld FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qld OCA], [https://pdbe.org/2qld PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qld RCSB], [https://www.ebi.ac.uk/pdbsum/2qld PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qld ProSAT]</span></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=2qld FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qld OCA], [https://pdbe.org/2qld PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qld RCSB], [https://www.ebi.ac.uk/pdbsum/2qld PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qld ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/DNJB1_HUMAN DNJB1_HUMAN]] Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP.  
[https://www.uniprot.org/uniprot/DNJB1_HUMAN DNJB1_HUMAN] Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP.
== 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=2qld 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=2qld ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
BACKGROUND: The mechanism by which Hsp40 and other molecular chaperones recognize and interact with non-native polypeptides is a fundamental question. How Hsp40 co-operates with Hsp70 to facilitate protein folding is not well understood. To investigate the mechanisms, we determined the crystal structure of the putative peptide-binding fragment of Hdj1, a human member of the type II Hsp40 family. RESULTS: The 2.7A structure reveals that Hdj1 forms a homodimer in the crystal by a crystallographic two-fold axis. The Hdj1 dimer has a U-shaped architecture and a large cleft is formed between the two elongated monomers. When compared with another Hsp40 Sis1 structure, the domain I of Hdj1 is rotated by 7.1 degree from the main body of the molecule, which makes the cleft between the two Hdj1 monomers smaller that that of Sis1. CONCLUSION: This structural observation indicates that the domain I of Hsp40 may possess significant flexibility. This flexibility may be important for Hsp40 to regulate the size of the cleft. We propose an "anchoring and docking" model for Hsp40 to utilize the flexibility of domain I to interact with non-native polypeptides and transfer them to Hsp70.
The crystal structure of the putative peptide-binding fragment from the human Hsp40 protein Hdj1.,Hu J, Wu Y, Li J, Qian X, Fu Z, Sha B BMC Struct Biol. 2008 Jan 22;8:3. PMID:18211704<ref>PMID:18211704</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2qld" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[DnaJ homolog 3D structures|DnaJ homolog 3D structures]]
*[[DnaJ homolog 3D structures|DnaJ homolog 3D structures]]
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Fu, Z]]
[[Category: Fu Z]]
[[Category: Hu, J]]
[[Category: Hu J]]
[[Category: Li, J]]
[[Category: Li J]]
[[Category: Sha, B]]
[[Category: Sha B]]
[[Category: Wu, Y]]
[[Category: Wu Y]]
[[Category: Chaperone]]
[[Category: Primarily beta sheet]]

Latest revision as of 12:16, 21 February 2024

human Hsp40 Hdj1human Hsp40 Hdj1

Structural highlights

2qld is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.7Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DNJB1_HUMAN Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP.

Evolutionary Conservation

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

See Also

2qld, resolution 2.70Å

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