1SQE
1.5A Crystal Structure Of the protein PG130 from Staphylococcus aureus, Structural genomics
1SQE の概要
| エントリーDOI | 10.2210/pdb1sqe/pdb |
| 分子名称 | hypothetical protein PG130 (2 entities in total) |
| 機能のキーワード | structural genomics, psi, protein structure initiative, midwest center for structural genomics, mcsg, unknown function |
| 由来する生物種 | Staphylococcus aureus |
| 細胞内の位置 | Cytoplasm (By similarity): Q99X56 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 25888.63 |
| 構造登録者 | Zhang, R.,Wu, R.,Joachimiak, G.,Schneewind, O.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (登録日: 2004-03-18, 公開日: 2004-08-03, 最終更新日: 2024-02-14) |
| 主引用文献 | Wu, R.,Skaar, E.P.,Zhang, R.,Joachimiak, G.,Gornicki, P.,Schneewind, O.,Joachimiak, A. Staphylococcus aureus IsdG and IsdI, heme-degrading enzymes with structural similarity to monooxygenases J.Biol.Chem., 280:2840-2846, 2005 Cited by PubMed Abstract: Heme-degrading enzymes are involved in human diseases ranging from stroke, cancer, and multiple sclerosis to infectious diseases such as malaria, diphtheria, and meningitis. All mammalian and microbial enzymes identified to date are members of the heme oxygenase superfamily and assume similar monomeric structures with an all alpha-helical fold. Here we describe the crystal structures of IsdG and IsdI, two heme-degrading enzymes from Staphylococcus aureus. The structures of both enzymes resemble the ferredoxin-like fold and form a beta-barrel at the dimer interface. Two large pockets found on the outside of the barrel contain the putative active sites. Sequence homologs of IsdG and IsdI were identified in multiple Gram-positive pathogens. Substitution of conserved IsdG amino acid residues either reduced or abolished heme degradation, suggesting a common catalytic mechanism. This mechanism of IsdG-mediated heme degradation may be similar to that of the structurally related monooxygenases, enzymes involved in the synthesis of antibiotics in Streptomyces. Our results imply the evolutionary adaptation of microbial enzymes to unique environments. PubMed: 15520015DOI: 10.1074/jbc.M409526200 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.5 Å) |
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