2z5i: Difference between revisions

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<StructureSection load='2z5i' size='340' side='right'caption='[[2z5i]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='2z5i' size='340' side='right'caption='[[2z5i]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2z5i]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z5I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Z5I FirstGlance]. <br>
<table><tr><td colspan='2'>[[2z5i]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z5I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Z5I FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=2z5i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z5i OCA], [https://pdbe.org/2z5i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2z5i RCSB], [https://www.ebi.ac.uk/pdbsum/2z5i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2z5i 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=2z5i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z5i OCA], [https://pdbe.org/2z5i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2z5i RCSB], [https://www.ebi.ac.uk/pdbsum/2z5i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2z5i ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/GCN4_YEAST GCN4_YEAST]] Is a transcription factor that is responsible for the activation of more than 30 genes required for amino acid or for purine biosynthesis in response to amino acid or purine starvation. Binds and recognize the DNA sequence: 5'-TGA[CG]TCA-3'. [[https://www.uniprot.org/uniprot/TPM1_RABIT TPM1_RABIT]] Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments.  
[https://www.uniprot.org/uniprot/GCN4_YEAST GCN4_YEAST] Is a transcription factor that is responsible for the activation of more than 30 genes required for amino acid or for purine biosynthesis in response to amino acid or purine starvation. Binds and recognize the DNA sequence: 5'-TGA[CG]TCA-3'.[https://www.uniprot.org/uniprot/TPM1_RABIT TPM1_RABIT] Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=2z5i ConSurf].
</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=2z5i ConSurf].
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<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Head-to-tail polymerization of tropomyosin is crucial for its actin binding, function in actin filament assembly, and the regulation of actin-myosin contraction. Here, we describe the 2.1 A resolution structure of crystals containing overlapping tropomyosin N and C termini (TM-N and TM-C) and the 2.9 A resolution structure of crystals containing TM-N and TM-C together with a fragment of troponin-T (TnT). At each junction, the N-terminal helices of TM-N were splayed, with only one of them packing against TM-C. In the C-terminal region of TM-C, a crucial water in the coiled-coil core broke the local 2-fold symmetry and helps generate a kink on one helix. In the presence of a TnT fragment, the asymmetry in TM-C facilitates formation of a 4-helix bundle containing two TM-C chains and one chain each of TM-N and TnT. Mutating the residues that generate the asymmetry in TM-C caused a marked decrease in the affinity of troponin for actin-tropomyosin filaments. The highly conserved region of TnT, in which most cardiomyopathy mutations reside, is crucial for interacting with tropomyosin. The structure of the ternary complex also explains why the skeletal- and cardiac-muscle specific C-terminal region is required to bind TnT and why tropomyosin homodimers bind only a single TnT. On actin filaments, the head-to-tail junction can function as a molecular swivel to accommodate irregularities in the coiled-coil path between successive tropomyosins enabling each to interact equivalently with the actin helix.
Structural basis for tropomyosin overlap in thin (actin) filaments and the generation of a molecular swivel by troponin-T.,Murakami K, Stewart M, Nozawa K, Tomii K, Kudou N, Igarashi N, Shirakihara Y, Wakatsuki S, Yasunaga T, Wakabayashi T Proc Natl Acad Sci U S A. 2008 May 20;105(20):7200-5. Epub 2008 May 15. PMID:18483193<ref>PMID:18483193</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2z5i" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Gcn4 3D Structures|Gcn4 3D Structures]]
*[[Gnc4 3D Structures|Gnc4 3D Structures]]
*[[Gnc4 3D Structures|Gnc4 3D Structures]]
*[[Tropomyosin|Tropomyosin]]
*[[Tropomyosin 3D structures|Tropomyosin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: European rabbit]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Igarashi, N]]
[[Category: Oryctolagus cuniculus]]
[[Category: Kudou, N]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Murakami, K]]
[[Category: Igarashi N]]
[[Category: Nozawa, K]]
[[Category: Kudou N]]
[[Category: Shirakihara, Y]]
[[Category: Murakami K]]
[[Category: Stewart, M]]
[[Category: Nozawa K]]
[[Category: Tomii, K]]
[[Category: Shirakihara Y]]
[[Category: Wakabayashi, T]]
[[Category: Stewart M]]
[[Category: Wakatsuki, S]]
[[Category: Tomii K]]
[[Category: Yasunaga, T]]
[[Category: Wakabayashi T]]
[[Category: Actin]]
[[Category: Wakatsuki S]]
[[Category: Cardiomyopathy]]
[[Category: Yasunaga T]]
[[Category: Contractile protein]]
[[Category: Cytoskeleton]]
[[Category: Tropomyosin]]
[[Category: Troponin]]

Latest revision as of 13:56, 13 March 2024

Crystal structure of the head-to-tail junction of tropomyosin

2z5i, resolution 2.10Å

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