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1g3i

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Revision as of 21:23, 24 December 2014

CRYSTAL STRUCTURE OF THE HSLUV PROTEASE-CHAPERONE COMPLEX

Structural highlights

1g3i is a 24 chain structure with sequence from Haemophilus influenzae. The August 2006 RCSB PDB Molecule of the Month feature on AAA+ Proteases by David S. Goodsell is 10.2210/rcsb_pdb/mom_2006_8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1g3k
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[HSLU_HAEIN] ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. [HSLV_HAEIN] Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.[HAMAP-Rule:MF_00248]

Evolutionary Conservation

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

Publication Abstract from PubMed

HslUV is a "prokaryotic proteasome" composed of the HslV protease and the HslU ATPase, a chaperone of the Clp/Hsp100 family. The 3.4 A crystal structure of an HslUV complex is presented here. Two hexameric ATP binding rings of HslU bind intimately to opposite sides of the HslV protease; the HslU "intermediate domains" extend outward from the complex. The solution structure of HslUV, derived from small angle X-ray scattering data under conditions where the complex is assembled and active, agrees with this crystallographic structure. When the complex forms, the carboxy-terminal helices of HslU distend and bind between subunits of HslV, and the apical helices of HslV shift substantially, transmitting a conformational change to the active site region of the protease.

Crystal and solution structures of an HslUV protease-chaperone complex.,Sousa MC, Trame CB, Tsuruta H, Wilbanks SM, Reddy VS, McKay DB Cell. 2000 Nov 10;103(4):633-43. PMID:11106733^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Sousa MC, Trame CB, Tsuruta H, Wilbanks SM, Reddy VS, McKay DB. Crystal and solution structures of an HslUV protease-chaperone complex. Cell. 2000 Nov 10;103(4):633-43. PMID:11106733

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1g3i"

@@ Line 7: / Line 7: @@
 <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=1g3i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g3i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1g3i RCSB], [http://www.ebi.ac.uk/pdbsum/1g3i PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/HSLU_HAEIN HSLU_HAEIN]] ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. [[http://www.uniprot.org/uniprot/HSLV_HAEIN HSLV_HAEIN]] Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.[HAMAP-Rule:MF_00248]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1g3i

From Proteopedia

Revision as of 21:23, 24 December 2014

CRYSTAL STRUCTURE OF THE HSLUV PROTEASE-CHAPERONE COMPLEX

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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