4cat
From Proteopedia
(New page: 200px<br /><applet load="4cat" size="450" color="white" frame="true" align="right" spinBox="true" caption="4cat, resolution 3.0Å" /> '''THREE-DIMENSIONAL STR...) |
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| - | [[Image:4cat.jpg|left|200px]]<br /><applet load="4cat" size=" | + | [[Image:4cat.jpg|left|200px]]<br /><applet load="4cat" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="4cat, resolution 3.0Å" /> | caption="4cat, resolution 3.0Å" /> | ||
'''THREE-DIMENSIONAL STRUCTURE OF CATALASE FROM PENICILLIUM VITALE AT 2.0 ANGSTROMS RESOLUTION'''<br /> | '''THREE-DIMENSIONAL STRUCTURE OF CATALASE FROM PENICILLIUM VITALE AT 2.0 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure analysis of crystalline fungal catalase | + | The three-dimensional structure analysis of crystalline fungal catalase from Penicillium vitale has been extended to 2.0 A resolution. The crystals belong to space group P3(1)21, with the unit cell parameters of a = b = 144.4 A and c = 133.8 A. The asymmetric unit contains half a tetrameric molecule of 222 symmetry. Each subunit is a single polypeptide chain of approximately 670 amino acid residues and binds one heme group. The amino acid sequence has been tentatively determined by computer graphics model building (using the FRODO system) and comparison with the known sequence of beef liver catalase. The atomic model has been refined by the Hendrickson & Konnert (1981) restrained least-squares program against 68,000 reflections between 5 A and 2 A resolution. The final R-factor is 0.31 after 24 refinement cycles. The secondary and tertiary structure of the catalase has been analyzed. |
==About this Structure== | ==About this Structure== | ||
| - | 4CAT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | + | 4CAT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=4CAT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Catalase]] | [[Category: Catalase]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Barynin, V | + | [[Category: Barynin, V V.]] |
| - | [[Category: Grebenko, A | + | [[Category: Grebenko, A I.]] |
| - | [[Category: Melik-Adamyan, W | + | [[Category: Melik-Adamyan, W R.]] |
| - | [[Category: Vagin, A | + | [[Category: Vagin, A A.]] |
| - | [[Category: Vainshtein, B | + | [[Category: Vainshtein, B K.]] |
[[Category: HEM]] | [[Category: HEM]] | ||
[[Category: oxidoreductase(h2o2(a))]] | [[Category: oxidoreductase(h2o2(a))]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:12:56 2008'' |
Revision as of 17:12, 21 February 2008
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THREE-DIMENSIONAL STRUCTURE OF CATALASE FROM PENICILLIUM VITALE AT 2.0 ANGSTROMS RESOLUTION
Overview
The three-dimensional structure analysis of crystalline fungal catalase from Penicillium vitale has been extended to 2.0 A resolution. The crystals belong to space group P3(1)21, with the unit cell parameters of a = b = 144.4 A and c = 133.8 A. The asymmetric unit contains half a tetrameric molecule of 222 symmetry. Each subunit is a single polypeptide chain of approximately 670 amino acid residues and binds one heme group. The amino acid sequence has been tentatively determined by computer graphics model building (using the FRODO system) and comparison with the known sequence of beef liver catalase. The atomic model has been refined by the Hendrickson & Konnert (1981) restrained least-squares program against 68,000 reflections between 5 A and 2 A resolution. The final R-factor is 0.31 after 24 refinement cycles. The secondary and tertiary structure of the catalase has been analyzed.
About this Structure
4CAT is a Protein complex structure of sequences from [1] with as ligand. Active as Catalase, with EC number 1.11.1.6 Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of catalase from Penicillium vitale at 2.0 A resolution., Vainshtein BK, Melik-Adamyan WR, Barynin VV, Vagin AA, Grebenko AI, Borisov VV, Bartels KS, Fita I, Rossmann MG, J Mol Biol. 1986 Mar 5;188(1):49-61. PMID:3712443
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