1mm4

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[[Image:1mm4.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1mm4", creates the "Structure Box" on the page.
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|GENE= CrcA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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{{STRUCTURE_1mm4| PDB=1mm4 | SCENE= }}
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|RELATEDENTRY=[[1mm5|1MM5]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mm4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mm4 OCA], [http://www.ebi.ac.uk/pdbsum/1mm4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mm4 RCSB]</span>
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'''Solution NMR structure of the outer membrane enzyme PagP in DPC micelles'''
'''Solution NMR structure of the outer membrane enzyme PagP in DPC micelles'''
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[[Category: Prive, G G.]]
[[Category: Prive, G G.]]
[[Category: Raetz, C R.H.]]
[[Category: Raetz, C R.H.]]
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[[Category: beta barrel]]
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[[Category: Beta barrel]]
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[[Category: palmitoyltransferase]]
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[[Category: Palmitoyltransferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:24:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:17:58 2008''
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Revision as of 22:24, 2 May 2008

Template:STRUCTURE 1mm4

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 Sat May 3 01:24:20 2008

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