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2dhr

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Revision as of 06:50, 10 November 2021

Whole cytosolic region of ATP-dependent metalloprotease FtsH (G399L)

Structural highlights

2dhr is a 6 chain structure with sequence from "flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1ixz, 1iy0, 1iy1, 1iy2
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[FTSH_THET8] Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins (By similarity).[HAMAP-Rule:MF_01458] Degrades preferentially unfolded substrates in a processive, ATP-dependent manner, usually after hydrophobic residues.[HAMAP-Rule:MF_01458]

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

An ATP-dependent protease, FtsH, digests misassembled membrane proteins in order to maintain membrane integrity and digests short-lived soluble proteins in order to control their cellular regulation. This enzyme has an N-terminal transmembrane segment and a C-terminal cytosolic region consisting of an AAA+ ATPase domain and a protease domain. Here we present two crystal structures: the protease domain and the whole cytosolic region. The cytosolic region fully retains an ATP-dependent protease activity and adopts a three-fold-symmetric hexameric structure. The protease domains displayed a six-fold symmetry, while the AAA+ domains, each containing ADP, alternate two orientations relative to the protease domain, making "open" and "closed" interdomain contacts. Apparently, ATPase is active only in the closed form, and protease operates in the open form. The protease catalytic sites are accessible only through a tunnel following from the AAA+ domain of the adjacent subunit, raising a possibility of translocation of polypeptide substrate to the protease sites through this tunnel.

Structure of the whole cytosolic region of ATP-dependent protease FtsH.,Suno R, Niwa H, Tsuchiya D, Zhang X, Yoshida M, Morikawa K Mol Cell. 2006 Jun 9;22(5):575-85. PMID:16762831^[1]

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

References

↑ Suno R, Niwa H, Tsuchiya D, Zhang X, Yoshida M, Morikawa K. Structure of the whole cytosolic region of ATP-dependent protease FtsH. Mol Cell. 2006 Jun 9;22(5):575-85. PMID:16762831 doi:10.1016/j.molcel.2006.04.020

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2dhr"

@@ Line 3: / Line 3: @@
 <StructureSection load='2dhr' size='340' side='right'caption='[[2dhr]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2dhr]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DHR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DHR FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2dhr]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DHR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DHR FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ixz|1ixz]], [[1iy0|1iy0]], [[1iy1|1iy1]], [[1iy2|1iy2]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ixz|1ixz]], [[1iy0|1iy0]], [[1iy1|1iy1]], [[1iy2|1iy2]]</div></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=2dhr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dhr OCA], [http://pdbe.org/2dhr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2dhr RCSB], [http://www.ebi.ac.uk/pdbsum/2dhr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2dhr 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=2dhr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dhr OCA], [https://pdbe.org/2dhr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dhr RCSB], [https://www.ebi.ac.uk/pdbsum/2dhr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dhr ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/FTSH_THET8 FTSH_THET8]] Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins (By similarity).[HAMAP-Rule:MF_01458]  Degrades preferentially unfolded substrates in a processive, ATP-dependent manner, usually after hydrophobic residues.[HAMAP-Rule:MF_01458]
+[[https://www.uniprot.org/uniprot/FTSH_THET8 FTSH_THET8]] Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins (By similarity).[HAMAP-Rule:MF_01458]  Degrades preferentially unfolded substrates in a processive, ATP-dependent manner, usually after hydrophobic residues.[HAMAP-Rule:MF_01458]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

2dhr

From Proteopedia

Revision as of 06:50, 10 November 2021

Whole cytosolic region of ATP-dependent metalloprotease FtsH (G399L)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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