We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1m85

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1m85.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1m85.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1m85| PDB=1m85 | SCENE= }}
{{STRUCTURE_1m85| PDB=1m85 | SCENE= }}
-
'''Structure of Proteus mirabilis catalase for the native form'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_7791219}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 7791219 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_7791219}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Jouve, H M.]]
[[Category: Jouve, H M.]]
[[Category: Methionine sulfone]]
[[Category: Methionine sulfone]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:45:11 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:25:12 2008''

Revision as of 20:25, 2 July 2008

Image:1m85.png

Template:STRUCTURE 1m85

Structure of Proteus mirabilis catalase for the native form

Template:ABSTRACT PUBMED 7791219

About this Structure

1M85 is a Single protein structure of sequence from Proteus mirabilis. This structure supersedes the now removed PDB entries and 1cae. 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 Wed Jul 2 23:25:12 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1m85"
Personal tools