1dlw

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(New page: 200px<br /> <applet load="1dlw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dlw, resolution 1.54&Aring;" /> '''X-RAY CRYSTAL STRUC...)
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[[Image:1dlw.gif|left|200px]]<br />
 
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<applet load="1dlw" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1dlw, resolution 1.54&Aring;" />
 
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'''X-RAY CRYSTAL STRUCTURE OF TRUNCATED HEMOGLOBIN FROM P.CAUDATUM.'''<br />
 
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==Overview==
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==X-RAY CRYSTAL STRUCTURE OF TRUNCATED HEMOGLOBIN FROM P.CAUDATUM.==
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Small hemoproteins displaying amino acid sequences 20-40 residues shorter, than (non-)vertebrate hemoglobins (Hbs) have recently been identified in, several pathogenic and non-pathogenic unicellular organisms, and named, 'truncated hemoglobins' (trHbs). They have been proposed to be involved, not only in oxygen transport but also in other biological functions, such, as protection against reactive nitrogen species, photosynthesis or to act, as terminal oxidases. Crystal structures of trHbs from the ciliated, protozoan Paramecium caudatum and the green unicellular alga Chlamydomonas, eugametos show that the tertiary structure of both proteins is based on a, 'two-over-two' alpha-helical sandwich, reflecting an unprecedented editing, of the classical 'three-over-three' alpha-helical globin fold. Based on, specific Gly-Gly motifs the tertiary structure accommodates the deletion, of the N-terminal A-helix and replacement of the crucial heme-binding, F-helix with an extended polypeptide loop. Additionally, concerted, structural modifications allow burying of the heme group and define the, distal site, which hosts a TyrB10, GlnE7 residue pair. A set of structural, and amino acid sequence consensus rules for stabilizing the fold and the, bound heme in the trHbs homology subfamily is deduced.
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<StructureSection load='1dlw' size='340' side='right'caption='[[1dlw]], [[Resolution|resolution]] 1.54&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1dlw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Paramecium_caudatum Paramecium caudatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DLW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DLW 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]] 1.54&#8491;</td></tr>
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<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>
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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=1dlw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dlw OCA], [https://pdbe.org/1dlw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dlw RCSB], [https://www.ebi.ac.uk/pdbsum/1dlw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dlw ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TRHBN_PARCA TRHBN_PARCA]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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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/dl/1dlw_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=1dlw ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1DLW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Paramecium_caudatum Paramecium caudatum] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DLW OCA].
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*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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A novel two-over-two alpha-helical sandwich fold is characteristic of the truncated hemoglobin family., Pesce A, Couture M, Dewilde S, Guertin M, Yamauchi K, Ascenzi P, Moens L, Bolognesi M, EMBO J. 2000 Jun 1;19(11):2424-34. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10835341 10835341]
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[[Category: Large Structures]]
[[Category: Paramecium caudatum]]
[[Category: Paramecium caudatum]]
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[[Category: Single protein]]
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[[Category: Bolognesi M]]
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[[Category: Bolognesi, M.]]
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[[Category: Couture M]]
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[[Category: Couture, M.]]
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[[Category: Dewilde S]]
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[[Category: Dewilde, S.]]
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[[Category: Guertin M]]
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[[Category: Guertin, M.]]
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[[Category: Moens L]]
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[[Category: Moens, L.]]
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[[Category: Pesce A]]
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[[Category: Pesce, A.]]
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[[Category: HEM]]
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[[Category: globin fold truncated hemoglobin non vertebrate hemoglobin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov 8 12:59:58 2007''
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Current revision

X-RAY CRYSTAL STRUCTURE OF TRUNCATED HEMOGLOBIN FROM P.CAUDATUM.

PDB ID 1dlw

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