This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1r1m

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1r1m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r1m, resolution 1.9&Aring;" /> '''Structure of the OmpA...)
Current revision (06:08, 17 April 2024) (edit) (undo)
 
(14 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1r1m.gif|left|200px]]<br /><applet load="1r1m" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1r1m, resolution 1.9&Aring;" />
 
-
'''Structure of the OmpA-like domain of RmpM from Neisseria meningitidis'''<br />
 
-
==Overview==
+
==Structure of the OmpA-like domain of RmpM from Neisseria meningitidis==
-
RmpM is a putative peptidoglycan binding protein from Neisseria, meningitidis that has been shown to interact with integral outer membrane, proteins such as porins and TonB-dependent transporters. Here we report, the 1.9 A crystal structure of the C-terminal domain of RmpM. The, 150-residue domain adopts a betaalphabetaalphabetabeta fold, as first, identified in Bacillus subtilis chorismate mutase. The C-terminal RmpM, domain is homologous to the periplasmic, C-terminal domain of Escherichia, coli OmpA; these domains are thought to be responsible for non-covalent, interactions with peptidoglycan. From the structure of the OmpA-like, domain of RmpM, we suggest a putative peptidoglycan binding site and, identify residues that may be essential for binding. Both the crystal, structure and solution experiments indicate that RmpM may exist as a, dimer. This would promote more efficient peptidoglycan binding, by, allowing RmpM to interact simultaneously with two glycan chains through, its C-terminal, OmpA-like binding domain, while its (structurally, uncharacterized) N-terminal domain could stabilize oligomers of porins and, TonB-dependent transporters in the outer membrane.
+
<StructureSection load='1r1m' size='340' side='right'caption='[[1r1m]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
-
 
+
== Structural highlights ==
-
==About this Structure==
+
<table><tr><td colspan='2'>[[1r1m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R1M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R1M FirstGlance]. <br>
-
1R1M 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 TRS as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1R1M OCA].
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
-
 
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
-
==Reference==
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1r1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r1m OCA], [https://pdbe.org/1r1m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r1m RCSB], [https://www.ebi.ac.uk/pdbsum/1r1m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r1m ProSAT]</span></td></tr>
-
Structure of the OmpA-like domain of RmpM from Neisseria meningitidis., Grizot S, Buchanan SK, Mol Microbiol. 2004 Feb;51(4):1027-37. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14763978 14763978]
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/OMP4_NEIMB OMP4_NEIMB]
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r1/1r1m_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1r1m ConSurf].
 +
<div style="clear:both"></div>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
[[Category: Neisseria meningitidis]]
[[Category: Neisseria meningitidis]]
-
[[Category: Single protein]]
+
[[Category: Buchanan SK]]
-
[[Category: Buchanan, S.K.]]
+
[[Category: Grizot S]]
-
[[Category: Grizot, S.]]
+
-
[[Category: TRS]]
+
-
[[Category: membrane protein]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:12:04 2007''
+

Current revision

Structure of the OmpA-like domain of RmpM from Neisseria meningitidis

PDB ID 1r1m

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools