1oap

From Proteopedia

(Difference between revisions)

Current revision

Mad structure of the periplasmique domain of the Escherichia coli PAL protein

Structural highlights

1oap is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.93Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PAL_ECOLI Thought to play a role in bacterial envelope integrity. Very strongly associated with the peptidoglycan.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The peptidoglycan-associated lipoprotein (Pal) from Escherichia coli is part of the Tol--Pal multiprotein complex used by group A colicins to penetrate and kill cells. Pal homologues are found in many Gram-negative bacteria and the Tol--Pal system is thought to play a role in bacterial envelope integrity. The Pal protein comprises 152 amino acids. Crystals of the C-terminal 109-amino-acid fragment of the Pal protein have been produced. The crystals belong to the tetragonal space group I4(1), with unit-cell parameters a = b = 89.3, c = 67.2 A. There are two molecules in the asymmetric unit. Frozen crystals diffract to at least 2.8 A resolution using synchrotron radiation. Selenomethionine-substituted truncated Pal protein is currently being produced in order to use multiwavelength anomalous dispersion (MAD) for phasing.

Crystallization and preliminary crystallographic study of the peptidoglycan-associated lipoprotein from Escherichia coli.,Abergel C, Walburger A, Chenivesse S, Lazdunski C Acta Crystallogr D Biol Crystallogr. 2001 Feb;57(Pt 2):317-9. PMID:11173492^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Abergel C, Walburger A, Chenivesse S, Lazdunski C. Crystallization and preliminary crystallographic study of the peptidoglycan-associated lipoprotein from Escherichia coli. Acta Crystallogr D Biol Crystallogr. 2001 Feb;57(Pt 2):317-9. PMID:11173492

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1oap"

@@ Line 3: / Line 3: @@
 <StructureSection load='1oap' size='340' side='right'caption='[[1oap]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1oap]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OAP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OAP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1oap]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OAP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OAP FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.93&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oap FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oap OCA], [http://pdbe.org/1oap PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1oap RCSB], [http://www.ebi.ac.uk/pdbsum/1oap PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1oap ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1oap FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oap OCA], [https://pdbe.org/1oap PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oap RCSB], [https://www.ebi.ac.uk/pdbsum/1oap PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oap ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PAL_ECOLI PAL_ECOLI]] Thought to play a role in bacterial envelope integrity. Very strongly associated with the peptidoglycan.
+[https://www.uniprot.org/uniprot/PAL_ECOLI PAL_ECOLI] Thought to play a role in bacterial envelope integrity. Very strongly associated with the peptidoglycan.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 35: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
 [[Category: Large Structures]]
-[[Category: Abergel, C]]
+[[Category: Abergel C]]
-[[Category: Bouveret, E]]
+[[Category: Bouveret E]]
-[[Category: Claverie, J M]]
+[[Category: Claverie JM]]
-[[Category: Walburger, A]]
+[[Category: Walburger A]]
-[[Category: Lipoprotein]]
-[[Category: Outer membrane]]
-[[Category: Peptidoglycan binding]]
-[[Category: Periplasmic]]
-[[Category: Tol system]]

1oap

From Proteopedia

Current revision

Mad structure of the periplasmique domain of the Escherichia coli PAL protein

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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