Loading
PDBj
メニューPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2GBB

Crystal structure of secreted chorismate mutase from Yersinia pestis

2GBB の概要
エントリーDOI10.2210/pdb2gbb/pdb
分子名称putative chorismate mutase, SULFATE ION, CITRIC ACID, ... (4 entities in total)
機能のキーワードalpha helical bundle, isomerase
由来する生物種Yersinia pestis biovar Microtus str. 91001
タンパク質・核酸の鎖数4
化学式量合計72871.24
構造登録者
Ladner, J.E.,Reddy, P.T.,Nelson, B.C.,Robinson, H.,Kim, S.-K. (登録日: 2006-03-10, 公開日: 2007-04-03, 最終更新日: 2024-10-30)
主引用文献Kim, S.K.,Reddy, S.K.,Nelson, B.C.,Robinson, H.,Reddy, P.T.,Ladner, J.E.
A comparative biochemical and structural analysis of the intracellular chorismate mutase (Rv0948c) from Mycobacterium tuberculosis H(37)R(v) and the secreted chorismate mutase (y2828) from Yersinia pestis.
Febs J., 275:4824-4835, 2008
Cited by
PubMed Abstract: The Rv0948c gene from Mycobacterium tuberculosis H(37)R(v) encodes a 90 amino acid protein as the natural gene product with chorismate mutase (CM) activity. The protein, 90-MtCM, exhibits Michaelis-Menten kinetics with a k(cat) of 5.5+/-0.2s(-1) and a K(m) of 1500+/-100microm at 37 degrees C and pH7.5. The 2.0A X-ray structure shows that 90-MtCM is an all alpha-helical homodimer (Protein Data Bank ID: 2QBV) with the topology of Escherichia coli CM (EcCM), and that both protomers contribute to each catalytic site. Superimposition onto the structure of EcCM and the sequence alignment shows that the C-terminus helix3 is shortened. The absence of two residues in the active site of 90-MtCM corresponding to Ser84 and Gln88 of EcCM appears to be one reason for the low k(cat). Hence, 90-MtCM belongs to a subfamily of alpha-helical AroQ CMs termed AroQ(delta.) The CM gene (y2828) from Yersinia pestis encodes a 186 amino acid protein with an N-terminal signal peptide that directs the protein to the periplasm. The mature protein, *YpCM, exhibits Michaelis-Menten kinetics with a k(cat) of 70+/-5s(-1) and K(m) of 500+/-50microm at 37 degrees C and pH7.5. The 2.1A X-ray structure shows that *YpCM is an all alpha-helical protein, and functions as a homodimer, and that each protomer has an independent catalytic unit (Protein Data Bank ID: 2GBB). *YpCM belongs to the AroQ(gamma) class of CMs, and is similar to the secreted CM (Rv1885c, *MtCM) from M.tuberculosis.
PubMed: 18727669
DOI: 10.1111/j.1742-4658.2008.06621.x
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.1 Å)
構造検証レポート
Validation report summary of 2gbb
検証レポート(詳細版)ダウンロードをダウンロード

249697

件を2026-02-25に公開中

PDB statisticsPDBj update infoContact PDBjnumon