2l4b: Difference between revisions

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 ==Solution structure of a putative acyl carrier protein from Anaplasma phagocytophilum. Seattle Structural Genomics Center for Infectious Disease target AnphA.01018.a==
-<StructureSection load='2l4b' size='340' side='right' caption='[[2l4b]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2l4b' size='340' side='right'caption='[[2l4b]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2l4b]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Anapz Anapz]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L4B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L4B FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2l4b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Anaplasma_phagocytophilum_str._HZ Anaplasma phagocytophilum str. HZ]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L4B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L4B FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">APH_0929 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=212042 ANAPZ])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2l4b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l4b OCA], [http://pdbe.org/2l4b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l4b RCSB], [http://www.ebi.ac.uk/pdbsum/2l4b PDBsum]</span></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=2l4b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l4b OCA], [https://pdbe.org/2l4b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l4b RCSB], [https://www.ebi.ac.uk/pdbsum/2l4b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l4b ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/Q2GJE9_ANAPZ Q2GJE9_ANAPZ]] Carrier of the growing fatty acid chain in fatty acid biosynthesis.[HAMAP-Rule:MF_01217][RuleBase:RU003545]
+[https://www.uniprot.org/uniprot/Q2GJE9_ANAPZ Q2GJE9_ANAPZ] Carrier of the growing fatty acid chain in fatty acid biosynthesis.[HAMAP-Rule:MF_01217][RuleBase:RU003545]
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The botulinum neurotoxins (BoNTs) produced by different strains of the bacterium Clostridium botulinum are responsible for the disease botulism and include a group of immunologically distinct serotypes (A, B, E, and F) that are considered to be the most lethal natural proteins known for humans. Two BoNT serotypes, C and D, while rarely associated with human infection, are responsible for deadly botulism outbreaks afflicting animals. Also associated with animal infections is the BoNT C-D mosaic protein (BoNT/CD), a BoNT subtype that is essentially a hybrid of the BoNT/C ( approximately two-third) and BoNT/D ( approximately one-third) serotypes. While the amino acid sequence of the heavy chain receptor binding (HCR) domain of BoNT/CD (BoNT/CD-HCR) is very similar to the corresponding amino acid sequence of BoNT/D, BoNT/CD-HCR binds synaptosome membranes better than BoNT/D-HCR. To obtain structural insights for the different membrane binding properties, the crystal structure of BoNT/CD-HCR (S867-E1280) was determined at 1.56A resolution and compared to previously reported structures for BoNT/D-HCR. Overall, the BoNT/CD-HCR structure is similar to the two sub-domain organization observed for other BoNT HCRs: an N-terminal jellyroll barrel motif and a C-terminal beta-trefoil fold. Comparison of the structure of BoNT/CD-HCR with BoNT/D-HCR indicates that K1118 has a similar structural role as the equivalent residue, E1114, in BoNT/D-HCR, while K1136 has a structurally different role than the equivalent residue, G1132, in BoNT/D-HCR. Lysine-1118 forms a salt bridge with E1247 and may enhance membrane interactions by stabilizing the putative membrane binding loop (K1240-N1248). Lysine-1136 is observed on the surface of the protein. A sulfate ion bound to K1136 may mimic a natural interaction with the negatively changed phospholipid membrane surface. Liposome-binding experiments demonstrate that BoNT/CD-HCR binds phosphatidylethanolamine liposomes more tightly than BoNT/D-HCR.
-Crystal structure of the receptor binding domain of the botulinum C-D mosaic neurotoxin reveals potential roles of lysines 1118 and 1136 in membrane interactions.,Zhang Y, Buchko GW, Qin L, Robinson H, Varnum SM Biochem Biophys Res Commun. 2011 Jan 7;404(1):407-12. Epub 2010 Dec 3. PMID:21130733<ref>PMID:21130733</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 2l4b" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Acyl carrier protein|Acyl carrier protein]]
+*[[Acyl carrier protein 3D structures|Acyl carrier protein 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Anapz]]
+[[Category: Anaplasma phagocytophilum str. HZ]]
-[[Category: Buchko, G W]]
+[[Category: Large Structures]]
-[[Category: Structural genomic]]
+[[Category: Buchko GW]]
-[[Category: Human granulocytic anaplasmosis]]
-[[Category: Infectious disease]]
-[[Category: Ssgcid]]
-[[Category: Transferase]]