1dgb

From Proteopedia

(Difference between revisions)

Revision as of 02:32, 10 September 2015

HUMAN ERYTHROCYTE CATALASE

Structural highlights

1dgb is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1dgf, 1dgg, 1dgh
Activity:	Catalase, with EC number 1.11.1.6
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

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.

Publication Abstract from PubMed

Human catalase is an heme-containing peroxisomal enzyme that breaks down hydrogen peroxide to water and oxygen; it is implicated in ethanol metabolism, inflammation, apoptosis, aging and cancer. The 1. 5 A resolution human enzyme structure, both with and without bound NADPH, establishes the conserved features of mammalian catalase fold and assembly, implicates Tyr370 as the tyrosine radical, suggests the structural basis for redox-sensitive binding of cognate mRNA via the catalase NADPH binding site, and identifies an unexpectedly substantial number of water-mediated domain contacts. A molecular ruler mechanism based on observed water positions in the 25 A-long channel resolves problems for selecting hydrogen peroxide. Control of water-mediated hydrogen bonds by this ruler selects for the longer hydrogen peroxide and explains the paradoxical effects of mutations that increase active site access but lower catalytic rate. The heme active site is tuned without compromising peroxide binding through a Tyr-Arg-His-Asp charge relay, arginine residue to heme carboxylate group hydrogen bonding, and aromatic stacking. Structures of the non-specific cyanide and specific 3-amino-1,2, 4-triazole inhibitor complexes of human catalase identify their modes of inhibition and help reveal the catalytic mechanism of catalase. Taken together, these resting state and inhibited human catalase structures support specific, structure-based mechanisms for the catalase substrate recognition, reaction and inhibition and provide a molecular basis for understanding ethanol intoxication and the likely effects of human polymorphisms.

Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism.,Putnam CD, Arvai AS, Bourne Y, Tainer JA J Mol Biol. 2000 Feb 11;296(1):295-309. PMID:10656833^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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
↑ 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
↑ Putnam CD, Arvai AS, Bourne Y, Tainer JA. Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism. J Mol Biol. 2000 Feb 11;296(1):295-309. PMID:10656833 doi:http://dx.doi.org/10.1006/jmbi.1999.3458

1 Structural highlights
2 Disease
3 Function
4 Evolutionary Conservation
5 Publication Abstract from PubMed
6 See Also
7 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1dgb"

@@ Line 6: / Line 6: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dgf|1dgf]], [[1dgg|1dgg]], [[1dgh|1dgh]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dgb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dgb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dgb RCSB], [http://www.ebi.ac.uk/pdbsum/1dgb PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dgb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dgb OCA], [http://pdbe.org/1dgb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dgb RCSB], [http://www.ebi.ac.uk/pdbsum/1dgb PDBsum]</span></td></tr>
 </table>
 == Disease ==
@@ Line 30: / Line 30: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1dgb" style="background-color:#fffaf0;"></div>
 ==See Also==

1dgb

From Proteopedia

Revision as of 02:32, 10 September 2015

HUMAN ERYTHROCYTE CATALASE

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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