2pi8

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (05:25, 17 October 2024) (edit) (undo)
 
(9 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2pi8.png|left|200px]]
 
-
<!--
+
==Crystal structure of E. coli MltA with bound chitohexaose==
-
The line below this paragraph, containing "STRUCTURE_2pi8", creates the "Structure Box" on the page.
+
<StructureSection load='2pi8' size='340' side='right'caption='[[2pi8]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[2pi8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PI8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PI8 FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-
{{STRUCTURE_2pi8| PDB=2pi8 | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2pi8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pi8 OCA], [https://pdbe.org/2pi8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pi8 RCSB], [https://www.ebi.ac.uk/pdbsum/2pi8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pi8 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/MLTA_ECOLI MLTA_ECOLI] Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division. Degrades murein glycan strands and insoluble, high-molecular weight murein sacculi.
 +
== 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/pi/2pi8_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2pi8 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Crystal structures of an inactive mutant (D308A) of the lytic transglycosylase MltA from Escherichia coli have been determined in two different apo-forms, as well as in complex with the substrate analogue chitohexaose. The chitohexaose binds with all six saccharide residues in the active site groove, with an intact glycosidic bond at the bond cleavage center. Its binding induces a large reorientation of the two structural domains in MltA, narrowing the active site groove and allowing tight interactions of the oligosaccharide with residues from both domains. The structures identify residues in MltA with key roles in the binding and recognition of peptidoglycan and confirm that Asp-308 is the single catalytic residue, acting as a general acid/base. Moreover, the structures suggest that catalysis involves a high energy conformation of the scissile glycosidic linkage and that the putative oxocarbenium ion intermediate is stabilized by the dipole moment of a nearby alpha-helix.
-
===Crystal structure of E. coli MltA with bound chitohexaose===
+
Structure of Escherichia coli Lytic transglycosylase MltA with bound chitohexaose: implications for peptidoglycan binding and cleavage.,van Straaten KE, Barends TR, Dijkstra BW, Thunnissen AM J Biol Chem. 2007 Jul 20;282(29):21197-205. Epub 2007 May 14. PMID:17502382<ref>PMID:17502382</ref>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<!--
+
</div>
-
The line below this paragraph, {{ABSTRACT_PUBMED_17502382}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 2pi8" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 17502382 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_17502382}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
[[Category: Escherichia coli K-12]]
-
[[2pi8]] is a 4 chain structure with 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=2PI8 OCA].
+
[[Category: Large Structures]]
-
 
+
[[Category: Barends TRM]]
-
==Reference==
+
[[Category: Dijkstra BW]]
-
<ref group="xtra">PMID:017502382</ref><references group="xtra"/>
+
[[Category: Thunnissen AMWH]]
-
[[Category: Escherichia coli]]
+
[[Category: Van Straaten KE]]
-
[[Category: Barends, T R.M.]]
+
-
[[Category: Dijkstra, B W.]]
+
-
[[Category: Straaten, K E.van.]]
+
-
[[Category: Thunnissen, A M.W H.]]
+
-
[[Category: Double-psi beta-barrel]]
+
-
[[Category: Hydrolase]]
+
-
[[Category: Lytic transglycosylase]]
+
-
[[Category: Protein-sugar complex]]
+

Current revision

Crystal structure of E. coli MltA with bound chitohexaose

PDB ID 2pi8

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools