1mm4
From Proteopedia
(New page: 200px<br /><applet load="1mm4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mm4" /> '''Solution NMR structure of the outer membrane...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1mm4.gif|left|200px]]<br /><applet load="1mm4" size=" | + | [[Image:1mm4.gif|left|200px]]<br /><applet load="1mm4" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mm4" /> | caption="1mm4" /> | ||
'''Solution NMR structure of the outer membrane enzyme PagP in DPC micelles'''<br /> | '''Solution NMR structure of the outer membrane enzyme PagP in DPC micelles'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The bacterial outer membrane enzyme PagP transfers a palmitate chain from | + | The bacterial outer membrane enzyme PagP transfers a palmitate chain from a phospholipid to lipid A. In a number of pathogenic Gram-negative bacteria, PagP confers resistance to certain cationic antimicrobial peptides produced during the host innate immune response. The global fold of Escherichia coli PagP was determined in both dodecylphosphocholine and n-octyl-beta-d-glucoside detergent micelles using solution NMR spectroscopy. PagP consists of an eight-stranded anti-parallel beta-barrel preceded by an amphipathic alpha helix. The beta-barrel is well defined, whereas NMR relaxation measurements reveal considerable mobility in the loops connecting individual beta-strands. Three amino acid residues critical for enzymatic activity localize to extracellular loops near the membrane interface, positioning them optimally to interact with the polar headgroups of lipid A. Hence, the active site of PagP is situated on the outer surface of the outer membrane. Because the phospholipids that donate palmitate in the enzymatic reaction are normally found only in the inner leaflet of the outer membrane, PagP activity may depend on the aberrant migration of phospholipids into the outer leaflet. This finding is consistent with an emerging paradigm for outer membrane enzymes in providing an adaptive response toward disturbances in the outer membrane. |
==About this Structure== | ==About this Structure== | ||
| - | 1MM4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 1MM4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MM4 OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bishop, R | + | [[Category: Bishop, R E.]] |
[[Category: Chen, L.]] | [[Category: Chen, L.]] | ||
| - | [[Category: Choy, W | + | [[Category: Choy, W Y.]] |
| - | [[Category: Forman-Kay, J | + | [[Category: Forman-Kay, J D.]] |
| - | [[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: Raetz, C | + | [[Category: Raetz, C R.H.]] |
[[Category: beta barrel]] | [[Category: beta barrel]] | ||
[[Category: palmitoyltransferase]] | [[Category: palmitoyltransferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:56:34 2008'' |
Revision as of 11:56, 21 February 2008
|
Solution NMR structure of the outer membrane enzyme PagP in DPC micelles
Overview
The bacterial outer membrane enzyme PagP transfers a palmitate chain from a phospholipid to lipid A. In a number of pathogenic Gram-negative bacteria, PagP confers resistance to certain cationic antimicrobial peptides produced during the host innate immune response. The global fold of Escherichia coli PagP was determined in both dodecylphosphocholine and n-octyl-beta-d-glucoside detergent micelles using solution NMR spectroscopy. PagP consists of an eight-stranded anti-parallel beta-barrel preceded by an amphipathic alpha helix. The beta-barrel is well defined, whereas NMR relaxation measurements reveal considerable mobility in the loops connecting individual beta-strands. Three amino acid residues critical for enzymatic activity localize to extracellular loops near the membrane interface, positioning them optimally to interact with the polar headgroups of lipid A. Hence, the active site of PagP is situated on the outer surface of the outer membrane. Because the phospholipids that donate palmitate in the enzymatic reaction are normally found only in the inner leaflet of the outer membrane, PagP activity may depend on the aberrant migration of phospholipids into the outer leaflet. This finding is consistent with an emerging paradigm for outer membrane enzymes in providing an adaptive response toward disturbances in the outer membrane.
About this Structure
1MM4 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Solution structure and dynamics of the outer membrane enzyme PagP by NMR., Hwang PM, Choy WY, Lo EI, Chen L, Forman-Kay JD, Raetz CR, Prive GG, Bishop RE, Kay LE, Proc Natl Acad Sci U S A. 2002 Oct 15;99(21):13560-5. Epub 2002 Sep 30. PMID:12357033
Page seeded by OCA on Thu Feb 21 13:56:34 2008
