1f4j: Difference between revisions

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-[[Image:1f4j.jpg|left|200px]]<br /><applet load="1f4j" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="1f4j, resolution 2.40&Aring;" />
-'''STRUCTURE OF TETRAGONAL CRYSTALS OF HUMAN ERYTHROCYTE CATALASE'''<br />
-==Overview==
+==STRUCTURE OF TETRAGONAL CRYSTALS OF HUMAN ERYTHROCYTE CATALASE==
-The structure of catalase from human erythrocytes (HEC) was determined in tetragonal crystals of space group I4(1) by molecular-replacement methods, using the orthorhombic crystal structure as a search model. It was then refined in a unit cell of dimensions a = b = 203.6 and c = 144.6 A, yielding R and R(free) of 0.196 and 0.244, respectively, for all data at 2.4 A resolution. A major difference of the HEC structure in the tetragonal crystal compared with the orthorhombic structure was the omission of a 20-residue N-terminal segment corresponding to the first exon of the human catalase gene. The overall structures were otherwise identical in both crystal forms. The NADPH-binding sites were empty in all four subunits and bound water molecules were observed at the active sites. The structure of the C-terminal segment, which corresponds to the last exon, remained undetermined. The tetragonal crystals showed a pseudo-4(1)22 symmetry in molecular packing. Two similar types of lattice contact interfaces between the HEC tetramers were observed; they were related by the pseudo-dyad axes.
+<StructureSection load='1f4j' size='340' side='right'caption='[[1f4j]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1f4j]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F4J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F4J 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]] 2.4&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=1f4j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f4j OCA], [https://pdbe.org/1f4j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f4j RCSB], [https://www.ebi.ac.uk/pdbsum/1f4j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f4j ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/CATA_HUMAN CATA_HUMAN] Defects in CAT are the cause of acatalasemia (ACATLAS) [MIM:[https://omim.org/entry/614097 614097]. A metabolic disorder characterized by absence of catalase activity in red cells and is often associated with ulcerating oral lesions.<ref>PMID:2308162</ref>
+== Function ==
+[https://www.uniprot.org/uniprot/CATA_HUMAN CATA_HUMAN] Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells and normal and transformed fibroblast cells.<ref>PMID:7882369</ref>
+== 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/f4/1f4j_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=1f4j ConSurf].
+<div style="clear:both"></div>
-==Disease==
+==See Also==
-Known disease associated with this structure: Acatalasemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=115500 115500]]
+*[[Catalase 3D structures|Catalase 3D structures]]
+== References ==
-==About this Structure==
+<references/>
-F4J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Catalase Catalase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.6 1.11.1.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F4J OCA].
+__TOC__
+</StructureSection>
-==Reference==
-Structure of tetragonal crystals of human erythrocyte catalase., Safo MK, Musayev FN, Wu SH, Abraham DJ, Ko TP, Acta Crystallogr D Biol Crystallogr. 2001 Jan;57(Pt 1):1-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11134921 11134921]
-[[Category: Catalase]]
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Abraham, D J.]]
+[[Category: Abraham DJ]]
-[[Category: Ko, T P.]]
+[[Category: Ko TP]]
-[[Category: Musayev, F N.]]
+[[Category: Musayev FN]]
-[[Category: Safo, M K.]]
+[[Category: Safo MK]]
-[[Category: Wu, S H.]]
+[[Category: Wu SH]]
-[[Category: HEM]]
-[[Category: heme protein]]
-[[Category: no bound nadph]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:34:45 2008''