1thq
From Proteopedia
(New page: 200px<br /><applet load="1thq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1thq, resolution 1.90Å" /> '''Crystal Structure of...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1thq.jpg|left|200px]]<br /><applet load="1thq" size=" | + | [[Image:1thq.jpg|left|200px]]<br /><applet load="1thq" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1thq, resolution 1.90Å" /> | caption="1thq, resolution 1.90Å" /> | ||
'''Crystal Structure of Outer Membrane Enzyme PagP'''<br /> | '''Crystal Structure of Outer Membrane Enzyme PagP'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The ability of enzymes to distinguish between fatty acyl groups can | + | The ability of enzymes to distinguish between fatty acyl groups can involve molecular measuring devices termed hydrocarbon rulers, but the molecular basis for acyl-chain recognition in any membrane-bound enzyme remains to be defined. PagP is an outer membrane acyltransferase that helps pathogenic bacteria to evade the host immune response by transferring a palmitate chain from a phospholipid to lipid A (endotoxin). PagP can distinguish lipid acyl chains that differ by a single methylene unit, indicating that the enzyme possesses a remarkably precise hydrocarbon ruler. We present the 1.9 A crystal structure of PagP, an eight-stranded beta-barrel with an unexpected interior hydrophobic pocket that is occupied by a single detergent molecule. The buried detergent is oriented normal to the presumed plane of the membrane, whereas the PagP beta-barrel axis is tilted by approximately 25 degrees. Acyl group specificity is modulated by mutation of Gly88 lining the bottom of the hydrophobic pocket, thus confirming the hydrocarbon ruler mechanism for palmitate recognition. A striking structural similarity between PagP and the lipocalins suggests an evolutionary link between these proteins. |
==About this Structure== | ==About this Structure== | ||
| - | 1THQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ACT, LDA and MPD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1THQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=LDA:'>LDA</scene> and <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1THQ OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Ahn, V | + | [[Category: Ahn, V E.]] |
| - | [[Category: Bishop, R | + | [[Category: Bishop, R E.]] |
[[Category: Chen, L.]] | [[Category: Chen, L.]] | ||
| - | [[Category: Engel, C | + | [[Category: Engel, C K.]] |
| - | [[Category: Hwang, P | + | [[Category: Hwang, P M.]] |
| - | [[Category: Kay, L | + | [[Category: Kay, L E.]] |
| - | [[Category: Lo, E | + | [[Category: Lo, E I.]] |
| - | [[Category: Prive, G | + | [[Category: Prive, G G.]] |
[[Category: ACT]] | [[Category: ACT]] | ||
[[Category: LDA]] | [[Category: LDA]] | ||
| Line 29: | Line 29: | ||
[[Category: palmitoyltransferase]] | [[Category: palmitoyltransferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:13:42 2008'' |
Revision as of 13:13, 21 February 2008
|
Crystal Structure of Outer Membrane Enzyme PagP
Overview
The ability of enzymes to distinguish between fatty acyl groups can involve molecular measuring devices termed hydrocarbon rulers, but the molecular basis for acyl-chain recognition in any membrane-bound enzyme remains to be defined. PagP is an outer membrane acyltransferase that helps pathogenic bacteria to evade the host immune response by transferring a palmitate chain from a phospholipid to lipid A (endotoxin). PagP can distinguish lipid acyl chains that differ by a single methylene unit, indicating that the enzyme possesses a remarkably precise hydrocarbon ruler. We present the 1.9 A crystal structure of PagP, an eight-stranded beta-barrel with an unexpected interior hydrophobic pocket that is occupied by a single detergent molecule. The buried detergent is oriented normal to the presumed plane of the membrane, whereas the PagP beta-barrel axis is tilted by approximately 25 degrees. Acyl group specificity is modulated by mutation of Gly88 lining the bottom of the hydrophobic pocket, thus confirming the hydrocarbon ruler mechanism for palmitate recognition. A striking structural similarity between PagP and the lipocalins suggests an evolutionary link between these proteins.
About this Structure
1THQ is a Single protein structure of sequence from Escherichia coli with , and as ligands. Full crystallographic information is available from OCA.
Reference
A hydrocarbon ruler measures palmitate in the enzymatic acylation of endotoxin., Ahn VE, Lo EI, Engel CK, Chen L, Hwang PM, Kay LE, Bishop RE, Prive GG, EMBO J. 2004 Aug 4;23(15):2931-41. Epub 2004 Jul 22. PMID:15272304
Page seeded by OCA on Thu Feb 21 15:13:42 2008
Categories: Escherichia coli | Single protein | Ahn, V E. | Bishop, R E. | Chen, L. | Engel, C K. | Hwang, P M. | Kay, L E. | Lo, E I. | Prive, G G. | ACT | LDA | MPD | Beta-barrel | Outer membrane enzyme | Pagp | Palmitoyltransferase
