1fhg: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1fhg.jpg|left|200px]]<br /><applet load="1fhg" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1fhg, resolution 2.0&Aring;" />
-'''HIGH RESOLUTION REFINEMENT OF TELOKIN'''<br />
-==Overview==
+==HIGH RESOLUTION REFINEMENT OF TELOKIN==
-The three-dimensional structure of telokin, an acidic protein identical to, the C-terminal portion of smooth muscle myosin light chain kinase from, turkey gizzard, has been determined at 2.8 A resolution and refined to a, crystallographic R-factor of 19.5% for all measured X-ray data from 30 A, to 2.8 A. Crystals used in the investigation belonged to the space group, P3(2)21, with one molecule per asymmetric unit and unit cell dimensions of, a = b = 64.4 A and c = 50.6 A. Telokin contains 154 amino acid residues, 103 of which were visible in the electron density map. The overall, molecular fold of telokin consists of seven strands of antiparallel, beta-pleated sheet that wrap around to form a barrel. There is also an, extended tail of eight amino acid residues at the N terminus that does not, participate in beta-sheet formation. The beta-barrel can be simply, envisioned as two layers of beta-sheet, nearly parallel to one another, with one layer containing four and the other three beta-strands. This type, of beta-barrel, as seen in telokin, was first observed for the CH2 domain, of an immunoglobulin fragment Fc. Telokin is an intracellular protein and, as such, does not contain the disulphide linkage between beta-strands B, and F normally observed in the immunoglobulin constant domains. It does, however, contain two cysteine amino acid residues (Cys63 and Cys115) that, are situated at structurally identical positions to those forming the, disulphide linkage in the immunoglobulin constant domain.
+<StructureSection load='1fhg' size='340' side='right'caption='[[1fhg]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1fhg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FHG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FHG FirstGlance]. <br>
+</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&#8491;</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=1fhg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fhg OCA], [https://pdbe.org/1fhg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fhg RCSB], [https://www.ebi.ac.uk/pdbsum/1fhg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fhg ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/MYLK_MELGA MYLK_MELGA] Corresponds to the C-terminus of smooth muscle myosin light chain kinase.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fh/1fhg_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1fhg ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The three-dimensional structure of telokin, an acidic protein identical to the C-terminal portion of smooth muscle myosin light chain kinase from turkey gizzard, has been determined at 2.8 A resolution and refined to a crystallographic R-factor of 19.5% for all measured X-ray data from 30 A to 2.8 A. Crystals used in the investigation belonged to the space group P3(2)21, with one molecule per asymmetric unit and unit cell dimensions of a = b = 64.4 A and c = 50.6 A. Telokin contains 154 amino acid residues, 103 of which were visible in the electron density map. The overall molecular fold of telokin consists of seven strands of antiparallel beta-pleated sheet that wrap around to form a barrel. There is also an extended tail of eight amino acid residues at the N terminus that does not participate in beta-sheet formation. The beta-barrel can be simply envisioned as two layers of beta-sheet, nearly parallel to one another, with one layer containing four and the other three beta-strands. This type of beta-barrel, as seen in telokin, was first observed for the CH2 domain of an immunoglobulin fragment Fc. Telokin is an intracellular protein and, as such, does not contain the disulphide linkage between beta-strands B and F normally observed in the immunoglobulin constant domains. It does, however, contain two cysteine amino acid residues (Cys63 and Cys115) that are situated at structurally identical positions to those forming the disulphide linkage in the immunoglobulin constant domain.
-==About this Structure==
+X-ray structure determination of telokin, the C-terminal domain of myosin light chain kinase, at 2.8 A resolution.,Holden HM, Ito M, Hartshorne DJ, Rayment I J Mol Biol. 1992 Oct 5;227(3):840-51. PMID:1404391<ref>PMID:1404391</ref>
-FHG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FHG OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-X-ray structure determination of telokin, the C-terminal domain of myosin light chain kinase, at 2.8 A resolution., Holden HM, Ito M, Hartshorne DJ, Rayment I, J Mol Biol. 1992 Oct 5;227(3):840-51. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1404391 1404391]
+</div>
+<div class="pdbe-citations 1fhg" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Meleagris gallopavo]]
-[[Category: Single protein]]
+[[Category: Kiyatkin A]]
-[[Category: Kiyatkin, A.]]
+[[Category: Lewinski K]]
-[[Category: Lewinski, K.]]
+[[Category: Minor W]]
-[[Category: Minor, W.]]
+[[Category: Somlyo AP]]
-[[Category: Somlyo, A.P.]]
+[[Category: Somlyo AV]]
-[[Category: Somlyo, A.V.]]
+[[Category: Tomchick DR]]
-[[Category: Tomchick, D.R.]]
-[[Category: beta barrel]]
-[[Category: immunoglobulin fold]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:55:33 2007''