1mqf
From Proteopedia
(New page: 200px<br /><applet load="1mqf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mqf, resolution 2.50Å" /> '''Compound I from Prot...) |
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| - | [[Image:1mqf.gif|left|200px]]<br /><applet load="1mqf" size=" | + | [[Image:1mqf.gif|left|200px]]<br /><applet load="1mqf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mqf, resolution 2.50Å" /> | caption="1mqf, resolution 2.50Å" /> | ||
'''Compound I from Proteus mirabilis catalase'''<br /> | '''Compound I from Proteus mirabilis catalase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of Proteus mirabilis catalase in complex with an inhibitor, formic acid, has been solved at 2.3 A resolution. Formic acid is a key | + | The structure of Proteus mirabilis catalase in complex with an inhibitor, formic acid, has been solved at 2.3 A resolution. Formic acid is a key ligand of catalase because of its ability to react with the ferric enzyme, giving a high-spin iron complex. Alternatively, it can react with two transient oxidized intermediates of the enzymatic mechanism, compounds I and II. In this work, the structures of native P. mirabilis catalase (PMC) and compound I have also been determined at high resolution (2.0 and 2.5 A, respectively) from frozen crystals. Comparisons between these three PMC structures show that a water molecule present at a distance of 3.5 A from the haem iron in the resting state is absent in the formic acid complex, but reappears in compound I. In addition, movements of solvent molecules are observed during formation of compound I in a cavity located away from the active site, in which a glycerol molecule is replaced by a sulfate. These results give structural insights into the movement of solvent molecules, which may be important in the enzymatic reaction. |
==About this Structure== | ==About this Structure== | ||
| - | 1MQF 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 SO4, O, HEM and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. This structure | + | 1MQF 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=O:'>O</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 entry 2CAF. 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=1MQF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Andreoletti, P.]] | [[Category: Andreoletti, P.]] | ||
[[Category: Gouet, P.]] | [[Category: Gouet, P.]] | ||
| - | [[Category: Jouve, H | + | [[Category: Jouve, H M.]] |
[[Category: Pernoud, A.]] | [[Category: Pernoud, A.]] | ||
[[Category: Sainz, G.]] | [[Category: Sainz, G.]] | ||
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[[Category: alpha + beta]] | [[Category: alpha + beta]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:57:59 2008'' |
Revision as of 11:58, 21 February 2008
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Compound I from Proteus mirabilis catalase
Overview
The structure of Proteus mirabilis catalase in complex with an inhibitor, formic acid, has been solved at 2.3 A resolution. Formic acid is a key ligand of catalase because of its ability to react with the ferric enzyme, giving a high-spin iron complex. Alternatively, it can react with two transient oxidized intermediates of the enzymatic mechanism, compounds I and II. In this work, the structures of native P. mirabilis catalase (PMC) and compound I have also been determined at high resolution (2.0 and 2.5 A, respectively) from frozen crystals. Comparisons between these three PMC structures show that a water molecule present at a distance of 3.5 A from the haem iron in the resting state is absent in the formic acid complex, but reappears in compound I. In addition, movements of solvent molecules are observed during formation of compound I in a cavity located away from the active site, in which a glycerol molecule is replaced by a sulfate. These results give structural insights into the movement of solvent molecules, which may be important in the enzymatic reaction.
About this Structure
1MQF is a Single protein structure of sequence from Proteus mirabilis with , , and as ligands. This structure supersedes the now removed PDB entry 2CAF. Active as Catalase, with EC number 1.11.1.6 Full crystallographic information is available from OCA.
Reference
Structural studies of Proteus mirabilis catalase in its ground state, oxidized state and in complex with formic acid., Andreoletti P, Pernoud A, Sainz G, Gouet P, Jouve HM, Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2163-8. Epub 2003, Nov 27. PMID:14646074
Page seeded by OCA on Thu Feb 21 13:57:59 2008
Categories: Catalase | Proteus mirabilis | Single protein | Andreoletti, P. | Gouet, P. | Jouve, H M. | Pernoud, A. | Sainz, G. | GOL | HEM | O | SO4 | Alpha + beta
