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[[Image:1qqw.gif|left|200px]]


{{Structure
==CRYSTAL STRUCTURE OF HUMAN ERYTHROCYTE CATALASE==
|PDB= 1qqw |SIZE=350|CAPTION= <scene name='initialview01'>1qqw</scene>, resolution 2.75&Aring;
<StructureSection load='1qqw' size='340' side='right'caption='[[1qqw]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene>
<table><tr><td colspan='2'>[[1qqw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The September 2004 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Catalase''  by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2004_9 10.2210/rcsb_pdb/mom_2004_9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QQW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QQW FirstGlance]. <br>
|ACTIVITY= [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]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75&#8491;</td></tr>
|GENE=  
<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=1qqw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qqw OCA], [https://pdbe.org/1qqw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qqw RCSB], [https://www.ebi.ac.uk/pdbsum/1qqw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qqw 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/qq/1qqw_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=1qqw ConSurf].
<div style="clear:both"></div>


'''CRYSTAL STRUCTURE OF HUMAN ERYTHROCYTE CATALASE'''
==See Also==
 
*[[Catalase|Catalase]]
 
*[[Catalase 3D structures|Catalase 3D structures]]
==Overview==
== References ==
Catalase (E.C. 1.11.1.6) was purified from human erythrocytes and crystallized in three different forms: orthorhombic, hexagonal and tetragonal. The structure of the orthorhombic crystal form of human erythrocyte catalase (HEC), with space group P2(1)2(1)2(1) and unit-cell parameters a = 84.9, b = 141.7, c = 232.5 A, was determined and refined with 2.75 A resolution data. Non-crystallographic symmetry restraints were employed and the resulting R value and R(free) were 0.206 and 0.272, respectively. The overall structure and arrangement of HEC molecules in the orthorhombic unit cell were very similar to those of bovine liver catalase (BLC). However, no NADPH was observed in the HEC crystal and a water was bound to the active-site residue His75. Conserved lattice interactions suggested a common growth mechanism for the orthorhombic crystals of HEC and BLC.
<references/>
 
__TOC__
==Disease==
</StructureSection>
Known disease associated with this structure: Acatalasemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=115500 115500]]
 
==About this Structure==
1QQW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The following page contains interesting information on the relation of 1QQW with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb57_1.html Catalase]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QQW OCA].
 
==Reference==
Structure of human erythrocyte catalase., Ko TP, Safo MK, Musayev FN, Di Salvo ML, Wang C, Wu SH, Abraham DJ, Acta Crystallogr D Biol Crystallogr. 2000 Feb;56(Pt 2):241-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10666617 10666617]
[[Category: Catalase]]
[[Category: Catalase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Abraham, D J.]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Ko, T P.]]
[[Category: Abraham DJ]]
[[Category: Musayev, F N.]]
[[Category: Ko TP]]
[[Category: Safo, M K.]]
[[Category: Musayev FN]]
[[Category: Wang, C.]]
[[Category: Safo MK]]
[[Category: Wu, S H.]]
[[Category: Wang C]]
[[Category: HEM]]
[[Category: Wu SH]]
[[Category: heme protein]]
[[Category: lattice contact]]
[[Category: no nadp]]
[[Category: water]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:41:28 2008''

Latest revision as of 11:16, 14 February 2024

CRYSTAL STRUCTURE OF HUMAN ERYTHROCYTE CATALASECRYSTAL STRUCTURE OF HUMAN ERYTHROCYTE CATALASE

Structural highlights

1qqw is a 4 chain structure with sequence from Homo sapiens. The September 2004 RCSB PDB Molecule of the Month feature on Catalase by David S. Goodsell is 10.2210/rcsb_pdb/mom_2004_9. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.75Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

CATA_HUMAN Defects in CAT are the cause of acatalasemia (ACATLAS) [MIM:614097. A metabolic disorder characterized by absence of catalase activity in red cells and is often associated with ulcerating oral lesions.[1]

Function

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.[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. Wen JK, Osumi T, Hashimoto T, Ogata M. Molecular analysis of human acatalasemia. Identification of a splicing mutation. J Mol Biol. 1990 Jan 20;211(2):383-93. PMID:2308162 doi:http://dx.doi.org/10.1016/0022-2836(90)90359-T
  2. Takeuchi A, Miyamoto T, Yamaji K, Masuho Y, Hayashi M, Hayashi H, Onozaki K. A human erythrocyte-derived growth-promoting factor with a wide target cell spectrum: identification as catalase. Cancer Res. 1995 Apr 1;55(7):1586-9. PMID:7882369

1qqw, resolution 2.75Å

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