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==Crystal structure of OmpA-like domain from Acinetobacter baumannii in complex with glycine==
==Crystal structure of OmpA-like domain from Acinetobacter baumannii in complex with glycine==
<StructureSection load='3td3' size='340' side='right' caption='[[3td3]], [[Resolution|resolution]] 1.59&Aring;' scene=''>
<StructureSection load='3td3' size='340' side='right'caption='[[3td3]], [[Resolution|resolution]] 1.59&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3td3]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Aciba Aciba]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TD3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TD3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3td3]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii Acinetobacter baumannii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TD3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TD3 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</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]] 1.59&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3td4|3td4]], [[3td5|3td5]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">omp38 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=470 ACIBA])</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=3td3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3td3 OCA], [https://pdbe.org/3td3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3td3 RCSB], [https://www.ebi.ac.uk/pdbsum/3td3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3td3 ProSAT]</span></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=3td3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3td3 OCA], [http://pdbe.org/3td3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3td3 RCSB], [http://www.ebi.ac.uk/pdbsum/3td3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3td3 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/OMP38_ACIBA OMP38_ACIBA]] Porin. Induces apoptosis in human laryngeal epithelial HEp-2 cells through caspases-dependent and AIF-dependent pathways. Purified Omp38 enters the cells and localizes to the mitochondria, which leads to a release of proapoptotic molecules such as cytochrome c and AIF (apoptosis-inducing factor).<ref>PMID:16008580</ref> <ref>PMID:9928952</ref>
[https://www.uniprot.org/uniprot/OMP38_ACIB2 OMP38_ACIB2] Functions as a porin (PubMed:9928952). Induces apoptosis in human cell lines through caspase-dependent and AIF-dependent pathways. Purified Omp38 enters host cell and localizes to the mitochondria, which presumably leads to a release of proapoptotic molecules such as cytochrome c and AIF (apoptosis-inducing factor) (PubMed:16008580). Binds peptidoglycan, contributes to cell wall maintenance (Probable).<ref>PMID:16008580</ref> <ref>PMID:9928952</ref> <ref>PMID:16008580</ref> <ref>PMID:21965596</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The outer membrane protein A (OmpA) plays important roles in anchoring of the outer membrane to the bacterial cell wall. The C-terminal periplasmic domain of OmpA (OmpA-like domain) associates with the peptidoglycan (PGN) layer noncovalently. However, there is a paucity of information on the structural aspects of the mechanism of PGN recognition by OmpA-like domains. To elucidate this molecular recognition process, we solved the high-resolution crystal structure of an OmpA-like domain from Acinetobacter baumannii bound to diaminopimelate (DAP), a unique bacterial amino acid from the PGN. The structure clearly illustrates that two absolutely conserved Asp271 and Arg286 residues are the key to the binding to DAP of PGN. Identification of DAP as the central anchoring site of PGN to OmpA is further supported by isothermal titration calorimetry and a pulldown assay with PGN. An NMR-based computational model for complexation between the PGN and OmpA emerged, and this model is validated by determining the crystal structure in complex with a synthetic PGN fragment. These structural data provide a detailed glimpse of how the anchoring of OmpA to the cell wall of gram-negative bacteria takes place in a DAP-dependent manner.-Park, J. S., Lee, W. C., Yeo, K. J., Ryu, K.-S., Kumarasiri, M., Hesek, D., Lee, M., Mobashery, S., Song, J. H., Lim, S. I., Lee, J. C., Cheong, C., Jeon, Y. H., Kim, H.-Y. Mechanism of anchoring of OmpA protein to the cell wall peptidoglycan of the gram-negative bacterial outer membrane.
 
Mechanism of anchoring of OmpA protein to the cell wall peptidoglycan of the gram-negative bacterial outer membrane.,Park JS, Lee WC, Yeo KJ, Ryu KS, Kumarasiri M, Hesek D, Lee M, Mobashery S, Song JH, Kim SI, Lee JC, Cheong C, Jeon YH, Kim HY FASEB J. 2011 Sep 30. PMID:21965596<ref>PMID:21965596</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3td3" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Aciba]]
[[Category: Acinetobacter baumannii]]
[[Category: Kim, H Y]]
[[Category: Large Structures]]
[[Category: Lee, W C]]
[[Category: Kim HY]]
[[Category: Park, J S]]
[[Category: Lee WC]]
[[Category: Song, J H]]
[[Category: Park JS]]
[[Category: Cell-wall attachment]]
[[Category: Song JH]]
[[Category: Membrane protein]]
[[Category: Ompa-like fold]]
[[Category: Peptide binding protein]]
[[Category: Peptidoglycan-binding]]

Latest revision as of 11:37, 20 March 2024

Crystal structure of OmpA-like domain from Acinetobacter baumannii in complex with glycineCrystal structure of OmpA-like domain from Acinetobacter baumannii in complex with glycine

Structural highlights

3td3 is a 8 chain structure with sequence from Acinetobacter baumannii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.59Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

OMP38_ACIB2 Functions as a porin (PubMed:9928952). Induces apoptosis in human cell lines through caspase-dependent and AIF-dependent pathways. Purified Omp38 enters host cell and localizes to the mitochondria, which presumably leads to a release of proapoptotic molecules such as cytochrome c and AIF (apoptosis-inducing factor) (PubMed:16008580). Binds peptidoglycan, contributes to cell wall maintenance (Probable).[1] [2] [3] [4]

References

  1. ↑ Choi CH, Lee EY, Lee YC, Park TI, Kim HJ, Hyun SH, Kim SA, Lee SK, Lee JC. Outer membrane protein 38 of Acinetobacter baumannii localizes to the mitochondria and induces apoptosis of epithelial cells. Cell Microbiol. 2005 Aug;7(8):1127-38. PMID:16008580 doi:CMI538
  2. ↑ Jyothisri K, Deepak V, Rajeswari MR. Purification and characterization of a major 40 kDa outer membrane protein of Acinetobacter baumannii. FEBS Lett. 1999 Jan 22;443(1):57-60. PMID:9928952
  3. ↑ Choi CH, Lee EY, Lee YC, Park TI, Kim HJ, Hyun SH, Kim SA, Lee SK, Lee JC. Outer membrane protein 38 of Acinetobacter baumannii localizes to the mitochondria and induces apoptosis of epithelial cells. Cell Microbiol. 2005 Aug;7(8):1127-38. PMID:16008580 doi:CMI538
  4. ↑ Park JS, Lee WC, Yeo KJ, Ryu KS, Kumarasiri M, Hesek D, Lee M, Mobashery S, Song JH, Kim SI, Lee JC, Cheong C, Jeon YH, Kim HY. Mechanism of anchoring of OmpA protein to the cell wall peptidoglycan of the gram-negative bacterial outer membrane. FASEB J. 2011 Sep 30. PMID:21965596 doi:10.1096/fj.11-188425

3td3, resolution 1.59Å

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