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1g41
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<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=1g41 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g41 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1g41 RCSB], [http://www.ebi.ac.uk/pdbsum/1g41 PDBsum]</span></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=1g41 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g41 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1g41 RCSB], [http://www.ebi.ac.uk/pdbsum/1g41 PDBsum]</span></td></tr> | ||
</table> | </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. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 16:44, 25 December 2014
CRYSTAL STRUCTURE OF HSLU HAEMOPHILUS INFLUENZAE
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