4eiw

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[[Image:4eiw.jpg|left|200px]]
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==Whole cytosolic region of atp-dependent metalloprotease FtsH (G399L)==
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<StructureSection load='4eiw' size='340' side='right' caption='[[4eiw]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4eiw]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EIW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EIW FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene><br>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ftsH, TTHA1492 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus])</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4eiw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eiw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4eiw RCSB], [http://www.ebi.ac.uk/pdbsum/4eiw PDBsum]</span></td></tr>
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<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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<ref>PMID:16762831</ref>
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The line below this paragraph, containing "STRUCTURE_4eiw", creates the "Structure Box" on the page.
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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or leave the SCENE parameter empty for the default display.
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{{STRUCTURE_4eiw| PDB=4eiw | SCENE= }}
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===Whole cytosolic region of atp-dependent metalloprotease FtsH (G399L)===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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The line below this paragraph, {{ABSTRACT_PUBMED_16762831}}, adds the Publication Abstract to the page
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__TOC__
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(as it appears on PubMed at http://www.pubmed.gov), where 16762831 is the PubMed ID number.
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</StructureSection>
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{{ABSTRACT_PUBMED_16762831}}
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==About this Structure==
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[[4eiw]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EIW OCA].
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==Reference==
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<ref group="xtra">PMID:016762831</ref><ref group="xtra">PMID:012377127</ref><references group="xtra"/>
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[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
[[Category: Morikawa, K.]]
[[Category: Morikawa, K.]]

Revision as of 07:31, 5 June 2014

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

4eiw, resolution 3.90Å

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