1m85
From Proteopedia
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| - | [[Image:1m85.gif|left|200px]]<br /> | + | [[Image:1m85.gif|left|200px]]<br /><applet load="1m85" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1m85" size=" | + | |
caption="1m85, resolution 2.00Å" /> | caption="1m85, resolution 2.00Å" /> | ||
'''Structure of Proteus mirabilis catalase for the native form'''<br /> | '''Structure of Proteus mirabilis catalase for the native form'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A catalase from a peroxide resistant mutant of Proteus mirabilis binds | + | 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== | ==About this Structure== | ||
| - | 1M85 is a | + | 1M85 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=SO4:'>SO4</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entries 2CAE and 1CAE. 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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M85 OCA]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7791219 7791219] | 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] | ||
| + | [[Category: Catalase]] | ||
[[Category: Proteus mirabilis]] | [[Category: Proteus mirabilis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Dideberg, O.]] | [[Category: Dideberg, O.]] | ||
[[Category: Gouet, P.]] | [[Category: Gouet, P.]] | ||
| - | [[Category: Jouve, H | + | [[Category: Jouve, H M.]] |
[[Category: GOL]] | [[Category: GOL]] | ||
[[Category: HEM]] | [[Category: HEM]] | ||
| Line 22: | Line 22: | ||
[[Category: methionine sulfone]] | [[Category: methionine sulfone]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:52:30 2008'' |
Revision as of 11:52, 21 February 2008
|
Structure of Proteus mirabilis catalase for the native form
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
1M85 is a Single protein structure of sequence from Proteus mirabilis with , and as ligands. This structure supersedes the now removed PDB entries 2CAE and 1CAE. Active as Catalase, with EC number 1.11.1.6 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 Thu Feb 21 13:52:30 2008
Categories: Catalase | Proteus mirabilis | Single protein | Dideberg, O. | Gouet, P. | Jouve, H M. | GOL | HEM | SO4 | Methionine sulfone
