8hq9
From Proteopedia
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(New page: '''Unreleased structure''' The entry 8hq9 is ON HOLD Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the MlaD domain of the MlaD protein from Escherichia coli (Form II)== | |
| - | + | <StructureSection load='8hq9' size='340' side='right'caption='[[8hq9]], [[Resolution|resolution]] 2.70Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[8hq9]] is a 6 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=8HQ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HQ9 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> | |
| - | [[Category: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO2:CARBON+DIOXIDE'>CO2</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=8hq9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hq9 OCA], [https://pdbe.org/8hq9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hq9 RCSB], [https://www.ebi.ac.uk/pdbsum/8hq9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hq9 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/MLAD_ECOLI MLAD_ECOLI] Part of the ABC transporter complex MlaFEDB, which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane (PubMed:19383799, PubMed:27529189). MlaD functions in substrate binding with strong affinity for phospholipids and modulates ATP hydrolytic activity of the complex (PubMed:27529189).<ref>PMID:19383799</ref> <ref>PMID:27529189</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli K-12]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Dutta A]] | ||
| + | [[Category: Kanaujia SP]] | ||
Current revision
Crystal structure of the MlaD domain of the MlaD protein from Escherichia coli (Form II)
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