Journal:Acta Cryst F:S2053230X21012632
From Proteopedia
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As expected, there is some conformational flexibility and differences between the <scene name='89/899477/Cv/3'>substrate-binding cavity</scene>, which explains substrate specificity. The substrate-binding cavity is labeled in royalblue. The superposed structures are PDB entry [[5jc8]] (apo structure of ''Px''SDR, whitesmoke), PDB entry [[1iy8]] (crystal structure of levodione reductase from ''Leifsonia aquatica'', red), PDB entry [[3ftp]] [3-ketoacyl-(acyl-carrier-protein) reductase from ''Burkholderia pseudomallei'', yellow], PDB entry [[6t6n]] [''Klebsiella pneumoniae'' | As expected, there is some conformational flexibility and differences between the <scene name='89/899477/Cv/3'>substrate-binding cavity</scene>, which explains substrate specificity. The substrate-binding cavity is labeled in royalblue. The superposed structures are PDB entry [[5jc8]] (apo structure of ''Px''SDR, whitesmoke), PDB entry [[1iy8]] (crystal structure of levodione reductase from ''Leifsonia aquatica'', red), PDB entry [[3ftp]] [3-ketoacyl-(acyl-carrier-protein) reductase from ''Burkholderia pseudomallei'', yellow], PDB entry [[6t6n]] [''Klebsiella pneumoniae'' | ||
FabG2(NADH-dependent) in complex with NADH, wheat] and PDB entry [[6ixm]] (ketone reductase ChKRED20 from the genome of ''Chryseobacterium'', aquamarine). The cofactor, NADH (magenta) and substrate, (4R)-2-methylpentane-2,4-diol (royalblue), are from PDB entry [[1iy8]]. Structures were superposed with ''PyMOL''. Uniquely, the <scene name='89/899477/Cv/4'>cofactor binding cavity</scene> of ''Px''SDR is not well conserved and differs from other SDRs. The cofactor-binding cavity is labeled in magenta. ''Px''SDR has an additional seven-amino acids that form an <scene name='89/899477/Cv/5'>additional unique loop</scene> within the co-factor binding cavity. Further studies are required to determine how these differences affect the enzymatic functions of the SDR. This project is an educational collaboration between the Seattle Structural Genomics Center for Infectious Disease (SSGCID) and Hampton University where undergraduate students are engaged in structure-function analysis and publication of structures solved by the SSGCID. | FabG2(NADH-dependent) in complex with NADH, wheat] and PDB entry [[6ixm]] (ketone reductase ChKRED20 from the genome of ''Chryseobacterium'', aquamarine). The cofactor, NADH (magenta) and substrate, (4R)-2-methylpentane-2,4-diol (royalblue), are from PDB entry [[1iy8]]. Structures were superposed with ''PyMOL''. Uniquely, the <scene name='89/899477/Cv/4'>cofactor binding cavity</scene> of ''Px''SDR is not well conserved and differs from other SDRs. The cofactor-binding cavity is labeled in magenta. ''Px''SDR has an additional seven-amino acids that form an <scene name='89/899477/Cv/5'>additional unique loop</scene> within the co-factor binding cavity. Further studies are required to determine how these differences affect the enzymatic functions of the SDR. This project is an educational collaboration between the Seattle Structural Genomics Center for Infectious Disease (SSGCID) and Hampton University where undergraduate students are engaged in structure-function analysis and publication of structures solved by the SSGCID. | ||
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| + | '''PDB reference:''' putative short-chain reductase, [[5jc8]]. | ||
<b>References</b><br> | <b>References</b><br> | ||
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![Structural and primary-sequence alignment of PxSDR with the closest structures identified by PDBeFold. Also shown is the percent identity matrix generated with Clustal2.1. The structures are PDB entry 5jc8 (the apo structure of PxSDR), PDB entry 1iy8 (the crystal structure of levodione reductase from Leifsonia aquatica), PDB entry 3ftp [3-ketoacyl-(acyl-carrier-protein) reductase from Burkholderia pseudomallei], PDB entry 6t6n [Klebsiella pneumoniae FabG2(NADH-dependent) in complex with NADH] and PDB entry 6ixm (ketone reductase ChKRED20 from the genome of Chryseobacterium). The secondary-structure elements shown are α-helices (α), 310-helices (η), β-strands (β) and β-turns (TT). Identical residues are shown in white on a red background and conserved residues are shown in red. This figure was generated using ESPript (Gouet et al., 1999, 2003),.](/wiki/index.php/Image:Figure2t1.png)
This page complements a publication in scientific journals and is one of the Proteopedia's Interactive 3D Complement pages. For aditional details please see I3DC.
