1qqw
From Proteopedia
(New page: 200px<br /> <applet load="1qqw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qqw, resolution 2.75Å" /> '''CRYSTAL STRUCTURE O...) |
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| - | [[Image:1qqw.gif|left|200px]]<br /> | + | [[Image:1qqw.gif|left|200px]]<br /><applet load="1qqw" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1qqw" size=" | + | |
caption="1qqw, resolution 2.75Å" /> | caption="1qqw, resolution 2.75Å" /> | ||
'''CRYSTAL STRUCTURE OF HUMAN ERYTHROCYTE CATALASE'''<br /> | '''CRYSTAL STRUCTURE OF HUMAN ERYTHROCYTE CATALASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Catalase (E.C. 1.11.1.6) was purified from human erythrocytes and | + | Catalase (E.C. 1.11.1.6) was purified from human erythrocytes and crystallized in three different forms: orthorhombic, hexagonal and tetragonal. The structure of the orthorhombic crystal form of human erythrocyte catalase (HEC), with space group P2(1)2(1)2(1) and unit-cell parameters a = 84.9, b = 141.7, c = 232.5 A, was determined and refined with 2.75 A resolution data. Non-crystallographic symmetry restraints were employed and the resulting R value and R(free) were 0.206 and 0.272, respectively. The overall structure and arrangement of HEC molecules in the orthorhombic unit cell were very similar to those of bovine liver catalase (BLC). However, no NADPH was observed in the HEC crystal and a water was bound to the active-site residue His75. Conserved lattice interactions suggested a common growth mechanism for the orthorhombic crystals of HEC and BLC. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QQW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. The following page contains interesting information on the relation of 1QQW with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb57_1.html Catalase]]. 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:// | + | 1QQW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. The following page contains interesting information on the relation of 1QQW with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb57_1.html Catalase]]. 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=1QQW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Abraham, D | + | [[Category: Abraham, D J.]] |
| - | [[Category: Ko, T | + | [[Category: Ko, T P.]] |
| - | [[Category: Musayev, F | + | [[Category: Musayev, F N.]] |
| - | [[Category: Safo, M | + | [[Category: Safo, M K.]] |
[[Category: Wang, C.]] | [[Category: Wang, C.]] | ||
| - | [[Category: Wu, S | + | [[Category: Wu, S H.]] |
[[Category: HEM]] | [[Category: HEM]] | ||
[[Category: heme protein]] | [[Category: heme protein]] | ||
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[[Category: water]] | [[Category: water]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:42:42 2008'' |
Revision as of 12:42, 21 February 2008
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CRYSTAL STRUCTURE OF HUMAN ERYTHROCYTE CATALASE
Contents |
Overview
Catalase (E.C. 1.11.1.6) was purified from human erythrocytes and crystallized in three different forms: orthorhombic, hexagonal and tetragonal. The structure of the orthorhombic crystal form of human erythrocyte catalase (HEC), with space group P2(1)2(1)2(1) and unit-cell parameters a = 84.9, b = 141.7, c = 232.5 A, was determined and refined with 2.75 A resolution data. Non-crystallographic symmetry restraints were employed and the resulting R value and R(free) were 0.206 and 0.272, respectively. The overall structure and arrangement of HEC molecules in the orthorhombic unit cell were very similar to those of bovine liver catalase (BLC). However, no NADPH was observed in the HEC crystal and a water was bound to the active-site residue His75. Conserved lattice interactions suggested a common growth mechanism for the orthorhombic crystals of HEC and BLC.
Disease
Known disease associated with this structure: Acatalasemia OMIM:[115500]
About this Structure
1QQW is a Single protein structure of sequence from Homo sapiens with as ligand. The following page contains interesting information on the relation of 1QQW with [Catalase]. Active as Catalase, with EC number 1.11.1.6 Full crystallographic information is available from OCA.
Reference
Structure of human erythrocyte catalase., Ko TP, Safo MK, Musayev FN, Di Salvo ML, Wang C, Wu SH, Abraham DJ, Acta Crystallogr D Biol Crystallogr. 2000 Feb;56(Pt 2):241-5. PMID:10666617
Page seeded by OCA on Thu Feb 21 14:42:42 2008
Categories: Catalase | Homo sapiens | Single protein | Abraham, D J. | Ko, T P. | Musayev, F N. | Safo, M K. | Wang, C. | Wu, S H. | HEM | Heme protein | Lattice contact | No nadp | Water
