2ciu

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[[Image:2ciu.jpg|left|200px]]
 
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==Structure of the IMS domain of the mitochondrial import protein Tim21 from S. cerevisiae==
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The line below this paragraph, containing "STRUCTURE_2ciu", creates the "Structure Box" on the page.
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<StructureSection load='2ciu' size='340' side='right'caption='[[2ciu]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2ciu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CIU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CIU FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ciu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ciu OCA], [https://pdbe.org/2ciu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ciu RCSB], [https://www.ebi.ac.uk/pdbsum/2ciu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ciu ProSAT]</span></td></tr>
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{{STRUCTURE_2ciu| PDB=2ciu | SCENE= }}
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</table>
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== Function ==
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'''STRUCTURE OF THE IMS DOMAIN OF THE MITOCHONDRIAL IMPORT PROTEIN TIM21 FROM S. CEREVISIAE'''
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[https://www.uniprot.org/uniprot/TIM21_YEAST TIM21_YEAST] Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. Required to keep the TOM and the TIM23 complexes in close contact. At some point, it is released from the TOM23 complex to allow protein translocation into the mitochondrial matrix. In the complex, it acts as an antagonist of TIM50 by reducing preprotein accumulation at the TOM23 complex and promotes dissociation of the PAM complex from the TIM23 complex.<ref>PMID:15797382</ref> <ref>PMID:15878866</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ci/2ciu_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2ciu ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
Proteins destined for the mitochondrial matrix are imported by the translocase of the outer membrane--the TOM complex--and the presequence translocase of the inner membrane--the TIM23 complex. At present, there is no structural information on components of the presequence translocase. Tim21, a subunit of the presequence translocase consisting of a membrane anchor and a carboxy-terminal domain exposed to the intermembrane space, directly connects the TOM and TIM23 complexes by binding to the intermembrane space domain of the Tom22 receptor. We crystallized the binding domain of Tim21 of Saccharomyces cerevisiae and determined its structure at 1.6 A resolution. The Tim21 structure represents a new alpha/beta-mixed protein fold with two alpha-helices flanked by an extended eight-stranded beta-sheet. We also identified a core sequence of Tom22 that binds to Tim21. Furthermore, negatively charged amino-acid residues of Tom22 are important for binding to Tim21. Here we suggest a mechanism for the TOM-TIM interaction.
Proteins destined for the mitochondrial matrix are imported by the translocase of the outer membrane--the TOM complex--and the presequence translocase of the inner membrane--the TIM23 complex. At present, there is no structural information on components of the presequence translocase. Tim21, a subunit of the presequence translocase consisting of a membrane anchor and a carboxy-terminal domain exposed to the intermembrane space, directly connects the TOM and TIM23 complexes by binding to the intermembrane space domain of the Tom22 receptor. We crystallized the binding domain of Tim21 of Saccharomyces cerevisiae and determined its structure at 1.6 A resolution. The Tim21 structure represents a new alpha/beta-mixed protein fold with two alpha-helices flanked by an extended eight-stranded beta-sheet. We also identified a core sequence of Tom22 that binds to Tim21. Furthermore, negatively charged amino-acid residues of Tom22 are important for binding to Tim21. Here we suggest a mechanism for the TOM-TIM interaction.
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==About this Structure==
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The Tim21 binding domain connects the preprotein translocases of both mitochondrial membranes.,Albrecht R, Rehling P, Chacinska A, Brix J, Cadamuro SA, Volkmer R, Guiard B, Pfanner N, Zeth K EMBO Rep. 2006 Dec;7(12):1233-8. Epub 2006 Nov 10. PMID:17099692<ref>PMID:17099692</ref>
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2CIU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CIU OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The Tim21 binding domain connects the preprotein translocases of both mitochondrial membranes., Albrecht R, Rehling P, Chacinska A, Brix J, Cadamuro SA, Volkmer R, Guiard B, Pfanner N, Zeth K, EMBO Rep. 2006 Dec;7(12):1233-8. Epub 2006 Nov 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17099692 17099692]
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</div>
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<div class="pdbe-citations 2ciu" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Albrecht R]]
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[[Category: Albrecht, R.]]
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[[Category: Pfanner N]]
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[[Category: Pfanner, N.]]
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[[Category: Rehling P]]
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[[Category: Rehling, P.]]
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[[Category: Zeth K]]
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[[Category: Zeth, K.]]
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[[Category: Inner membrane]]
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[[Category: Membrane]]
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[[Category: Mitochondrial import]]
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[[Category: Mitochondrion]]
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[[Category: Protein transport]]
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[[Category: Transit peptide]]
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[[Category: Translocation]]
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[[Category: Transmembrane]]
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[[Category: Transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 22:15:02 2008''
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Current revision

Structure of the IMS domain of the mitochondrial import protein Tim21 from S. cerevisiae

PDB ID 2ciu

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