1k24: Difference between revisions

Revision as of 14:29, 21 February 2008

Crystal Structure of the OpcA Outer Membrane Adhesin/Invasin from Neisseria meningitidis

OverviewOverview

OpcA is an integral outer membrane protein from Neisseria meningitidis, the causative agent of meningococcal meningitis and septicemia. It mediates the adhesion of N. meningitidis to epithelial and endothelial cells by binding to vitronectin and proteoglycan cell-surface receptors. Here, we report the determination of the crystal structure of OpcA to 2.0 A resolution. OpcA adopts a 10-stranded beta-barrel structure with extensive loop regions that protrude above the predicted surface of the membrane. The second external loop adopts an unusual conformation, traversing the axis of the beta-barrel and apparently blocking formation of a pore through the membrane. Loops 2, 3, 4, and 5 associate to form one side of a crevice in the external surface of the structure, the other side being formed by loop 1. The crevice is lined by positively charged residues and would form an ideal binding site for proteoglycan polysaccharide. The structure, therefore, suggests a model for how adhesion of this important human pathogen to proteoglycan is mediated at the molecular level.

About this StructureAbout this Structure

1K24 is a Single protein structure of sequence from Neisseria meningitidis with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the OpcA integral membrane adhesin from Neisseria meningitidis., Prince SM, Achtman M, Derrick JP, Proc Natl Acad Sci U S A. 2002 Mar 19;99(6):3417-21. Epub 2002 Mar 12. PMID:11891340

Page seeded by OCA on Thu Feb 21 13:29:15 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1k24.jpg|left|200px]]<br /><applet load="1k24" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1k24.jpg|left|200px]]<br /><applet load="1k24" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1k24, resolution 2.03&Aring;" />
 '''Crystal Structure of the OpcA Outer Membrane Adhesin/Invasin from Neisseria meningitidis'''<br />
 ==Overview==
-OpcA is an integral outer membrane protein from Neisseria meningitidis, the causative agent of meningococcal meningitis and septicemia. It, mediates the adhesion of N. meningitidis to epithelial and endothelial, cells by binding to vitronectin and proteoglycan cell-surface receptors., Here, we report the determination of the crystal structure of OpcA to 2.0, A resolution. OpcA adopts a 10-stranded beta-barrel structure with, extensive loop regions that protrude above the predicted surface of the, membrane. The second external loop adopts an unusual conformation, traversing the axis of the beta-barrel and apparently blocking formation, of a pore through the membrane. Loops 2, 3, 4, and 5 associate to form one, side of a crevice in the external surface of the structure, the other side, being formed by loop 1. The crevice is lined by positively charged, residues and would form an ideal binding site for proteoglycan, polysaccharide. The structure, therefore, suggests a model for how, adhesion of this important human pathogen to proteoglycan is mediated at, the molecular level.
+OpcA is an integral outer membrane protein from Neisseria meningitidis, the causative agent of meningococcal meningitis and septicemia. It mediates the adhesion of N. meningitidis to epithelial and endothelial cells by binding to vitronectin and proteoglycan cell-surface receptors. Here, we report the determination of the crystal structure of OpcA to 2.0 A resolution. OpcA adopts a 10-stranded beta-barrel structure with extensive loop regions that protrude above the predicted surface of the membrane. The second external loop adopts an unusual conformation, traversing the axis of the beta-barrel and apparently blocking formation of a pore through the membrane. Loops 2, 3, 4, and 5 associate to form one side of a crevice in the external surface of the structure, the other side being formed by loop 1. The crevice is lined by positively charged residues and would form an ideal binding site for proteoglycan polysaccharide. The structure, therefore, suggests a model for how adhesion of this important human pathogen to proteoglycan is mediated at the molecular level.
 ==About this Structure==
-K24 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis] with ZN and 1PE as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1K24 OCA].
+K24 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=1PE:'>1PE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K24 OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Achtman, M.]]
-[[Category: Derrick, J.P.]]
+[[Category: Derrick, J P.]]
-[[Category: Prince, S.M.]]
+[[Category: Prince, S M.]]
 [[Category: 1PE]]
 [[Category: ZN]]
@@ Line 24: / Line 24: @@
 [[Category: outer membrane]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 00:35:05 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:29:15 2008''