2cah

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[[Image:2cah.gif|left|200px]]<br /><applet load="2cah" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2cah.gif|left|200px]]
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caption="2cah, resolution 2.7&Aring;" />
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'''STRUCTURE OF PROTEUS MIRABILIS PR CATALASE FOR THE NATIVE FORM (E-FE(III)) COMPLEXED WITH NADPH'''<br />
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{{Structure
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|PDB= 2cah |SIZE=350|CAPTION= <scene name='initialview01'>2cah</scene>, resolution 2.7&Aring;
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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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|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=NDP:NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE'>NDP</scene>
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|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]
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|GENE=
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}}
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'''STRUCTURE OF PROTEUS MIRABILIS PR CATALASE FOR THE NATIVE FORM (E-FE(III)) COMPLEXED WITH NADPH'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2CAH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Proteus_mirabilis Proteus mirabilis] with <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=NDP:'>NDP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1CAF. 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] Known structural/functional Sites: <scene name='pdbsite=337:Proximal+TYR'>337</scene> and <scene name='pdbsite=54:Distal+HIS'>54</scene>. 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 1CAF. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CAH OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7791219 7791219]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/7791219 7791219]
[[Category: Catalase]]
[[Category: Catalase]]
[[Category: Proteus mirabilis]]
[[Category: Proteus mirabilis]]
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[[Category: peroxidase]]
[[Category: peroxidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:46:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:12:57 2008''

Revision as of 14:12, 20 March 2008


PDB ID 2cah

Drag the structure with the mouse to rotate
, resolution 2.7Å
Sites: and
Ligands: and
Activity: Catalase, with EC number 1.11.1.6
Coordinates: save as pdb, mmCIF, xml



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

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