1hl5: Difference between revisions
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==Overview== | ==Overview== | ||
Cu, Zn superoxide dismutase (SOD1) forms a crucial component of the, cellular defence against oxidative stress. Zn-deficient wild-type and, mutant human SOD1 have been implicated in the disease familial amyotrophic, lateral sclerosis (FALS). We present here the crystal structures of holo, and metal-deficient (apo) wild-type protein at 1.8A resolution. The P21, wild-type holo enzyme structure has nine independently refined dimers and, these combine to form a "trimer of dimers" packing motif in each, asymmetric unit. There is no significant asymmetry between the monomers in, these dimers, in contrast to the subunit structures of the FALS G37R, mutant of human SOD1 and in bovine Cu,Zn SOD. Metal-deficient apo SOD1, crystallizes with two dimers in the asymmetric unit and shows changes in, the ... | Cu, Zn superoxide dismutase (SOD1) forms a crucial component of the, cellular defence against oxidative stress. Zn-deficient wild-type and, mutant human SOD1 have been implicated in the disease familial amyotrophic, lateral sclerosis (FALS). We present here the crystal structures of holo, and metal-deficient (apo) wild-type protein at 1.8A resolution. The P21, wild-type holo enzyme structure has nine independently refined dimers and, these combine to form a "trimer of dimers" packing motif in each, asymmetric unit. There is no significant asymmetry between the monomers in, these dimers, in contrast to the subunit structures of the FALS G37R, mutant of human SOD1 and in bovine Cu,Zn SOD. Metal-deficient apo SOD1, crystallizes with two dimers in the asymmetric unit and shows changes in, the metal-binding sites and disorder in the Zn binding and electrostatic, loops of one dimer, which is devoid of metals. The second dimer lacks Cu, but has approximately 20% occupancy of the Zn site and remains, structurally similar to wild-type SOD1. The apo protein forms a, continuous, extended arrangement of beta-barrels stacked up along the, short crystallographic b-axis, while perpendicular to this axis, the, constituent beta-strands form a zig-zag array of filaments, the overall, arrangement of which has a similarity to the common structure associated, with amyloid-like fibrils. | ||
==About this Structure== | ==About this Structure== | ||
1HL5 is a | 1HL5 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 CU, ZN and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HL5 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: zn superoxide dismutase]] | [[Category: zn superoxide dismutase]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 15:31:22 2007'' | ||
