1yzr
From Proteopedia
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| - | [[Image:1yzr.gif|left|200px]] | + | [[Image:1yzr.gif|left|200px]] |
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| - | '''Manganese peroxidase-Sm(III) complex''' | + | {{Structure |
| + | |PDB= 1yzr |SIZE=350|CAPTION= <scene name='initialview01'>1yzr</scene>, resolution 1.6Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SM:SAMARIUM+(III)+ION'>SM</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Manganese_peroxidase Manganese peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.13 1.11.1.13] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Manganese peroxidase-Sm(III) complex''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1YZR is a [ | + | 1YZR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Phanerochaete_chrysosporium Phanerochaete chrysosporium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YZR OCA]. |
==Reference== | ==Reference== | ||
| - | High-resolution crystal structure of manganese peroxidase: substrate and inhibitor complexes., Sundaramoorthy M, Youngs HL, Gold MH, Poulos TL, Biochemistry. 2005 May 3;44(17):6463-70. PMID:[http:// | + | High-resolution crystal structure of manganese peroxidase: substrate and inhibitor complexes., Sundaramoorthy M, Youngs HL, Gold MH, Poulos TL, Biochemistry. 2005 May 3;44(17):6463-70. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15850380 15850380] |
[[Category: Manganese peroxidase]] | [[Category: Manganese peroxidase]] | ||
[[Category: Phanerochaete chrysosporium]] | [[Category: Phanerochaete chrysosporium]] | ||
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[[Category: peroxidase]] | [[Category: peroxidase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:29:30 2008'' |
Revision as of 13:29, 20 March 2008
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| , resolution 1.6Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , and | ||||||
| Activity: | Manganese peroxidase, with EC number 1.11.1.13 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Manganese peroxidase-Sm(III) complex
Overview
Manganese peroxidase (MnP) is an extracellular heme enzyme that catalyzes the peroxide-dependent oxidation of Mn(II) to Mn(III). The Mn(III) is released from the enzyme in complex with oxalate. One heme propionate and the side chains of Glu35, Glu39, and Asp179 were identified as Mn(II) ligands in the 2.0 A resolution crystal structure. The new 1.45 A crystal structure of MnP complexed with Mn(II) provides a more accurate view of the Mn-binding site. New features include possible partial protonation of Glu39 in the Mn-binding site and glycosylation at Ser336. This is also the first report of MnP-inhibitor complex structures. At the Mn-binding site, divalent Cd(II) exhibits octahedral, hexacoordinate ligation geometry similar to that of Mn(II). Cd(II) also binds to a putative second weak metal-binding site with tetrahedral geometry at the C-terminus of the protein. Unlike that for Mn(II) and Cd(II), coordination of trivalent Sm(III) at the Mn-binding site is octacoordinate. Sm(III) was removed from a MnP-Sm(III) crystal by soaking the crystal in oxalate and then reintroduced into the binding site. Thus, direct comparisons of Sm(III)-bound and metal-free structures were made using the same crystal. No ternary complex was observed upon incubation with oxalate. The reversible binding of Sm(III) may be a useful model for the reversible binding of Mn(III) to the enzyme, which is too unstable to allow similar examination.
About this Structure
1YZR is a Single protein structure of sequence from Phanerochaete chrysosporium. Full crystallographic information is available from OCA.
Reference
High-resolution crystal structure of manganese peroxidase: substrate and inhibitor complexes., Sundaramoorthy M, Youngs HL, Gold MH, Poulos TL, Biochemistry. 2005 May 3;44(17):6463-70. PMID:15850380
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