2cah

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[[Image:2cah.gif|left|200px]]
[[Image:2cah.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2cah |SIZE=350|CAPTION= <scene name='initialview01'>2cah</scene>, resolution 2.7&Aring;
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The line below this paragraph, containing "STRUCTURE_2cah", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=337:Proximal+TYR'>337</scene> and <scene name='pdbsite=54:Distal+HIS'>54</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=OMT:S-DIOXYMETHIONINE'>OMT</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <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>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_2cah| PDB=2cah | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cah OCA], [http://www.ebi.ac.uk/pdbsum/2cah PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2cah RCSB]</span>
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}}
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'''STRUCTURE OF PROTEUS MIRABILIS PR CATALASE FOR THE NATIVE FORM (E-FE(III)) COMPLEXED WITH NADPH'''
'''STRUCTURE OF PROTEUS MIRABILIS PR CATALASE FOR THE NATIVE FORM (E-FE(III)) COMPLEXED WITH NADPH'''
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==About this Structure==
==About this Structure==
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2CAH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Proteus_mirabilis Proteus mirabilis]. This structure supersedes the now removed PDB entry 1CAF. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CAH OCA].
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2CAH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Proteus_mirabilis Proteus mirabilis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1caf 1caf]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CAH OCA].
==Reference==
==Reference==
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[[Category: Gouet, P.]]
[[Category: Gouet, P.]]
[[Category: Jouve, H M.]]
[[Category: Jouve, H M.]]
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[[Category: oxidoreductase (h2o2 acceptor)]]
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[[Category: Peroxidase]]
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[[Category: peroxidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:34:42 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:18:46 2008''
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Revision as of 18:34, 3 May 2008

Template:STRUCTURE 2cah

STRUCTURE OF PROTEUS MIRABILIS PR CATALASE FOR THE NATIVE FORM (E-FE(III)) COMPLEXED WITH NADPH


Overview

A catalase from a peroxide resistant mutant of Proteus mirabilis binds NADPH tightly. Interestingly, this enzyme can be stripped of NADPH without loss of the catalatic activity. It is the only known non-mammalian catalase able to bind NADPH. The structure without cofactor was solved by molecular replacement using the structure of beef liver catalase as a model. The structure was refined to an R-factor of 19.3% in the range 8 to 2.2 A resolution. According to the sequence, a methionine sulphone was positioned in the haem active site. This oxidized form of methionine is particular to Proteus mirabilis catalase and likely to produce some steric hindrance in the active site. Two important water molecules are positioned in the haem distal site. These two water molecules are not located in the structure of beef liver catalase, but are supposed to account for the catalytic mechanism. The liganded form was obtained by soaking crystals of the unliganded form into an NADPH solution. The structure was refined to an R-factor of 15.9% in the range of 8 to 3.1 A resolution using the unliganded structure as a model. The NADPH was clearly located in the electron density map with the same conformation as in beef liver catalase. The NADPH binding induces slight structural changes. However, the imidazole ring of a histidine residue (His284) rotates about 50 degrees to accommodate the cofactor. The electron transfer from NADPH to the haem molecule was examined and several pathways are proposed.

About this Structure

2CAH is a Single protein structure of sequence from Proteus mirabilis. This structure supersedes the now removed PDB entry 1caf. Full crystallographic information is available from OCA.

Reference

Crystal structure of Proteus mirabilis PR catalase with and without bound NADPH., Gouet P, Jouve HM, Dideberg O, J Mol Biol. 1995 Jun 23;249(5):933-54. PMID:7791219 Page seeded by OCA on Sat May 3 21:34:42 2008

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