5hbc
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 5hbc is ON HOLD Authors: Singh, A., Rastogi, N., Singh, P.K., Tyagi, T.K., Kaur, P., Sharma, S., Singh, T.P. Description: Intermediate structure of...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Intermediate structure of iron-saturated C-lobe of bovine lactoferrin at 2.79 Angstrom resolution indicates the softening of iron coordination== | |
| + | <StructureSection load='5hbc' size='340' side='right'caption='[[5hbc]], [[Resolution|resolution]] 2.79Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5hbc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HBC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HBC 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]] 2.79Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCT:BICARBONATE+ION'>BCT</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=5hbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hbc OCA], [https://pdbe.org/5hbc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hbc RCSB], [https://www.ebi.ac.uk/pdbsum/5hbc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hbc ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/TRFL_BOVIN TRFL_BOVIN] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate.<ref>PMID:8980754</ref> <ref>PMID:15222473</ref> Lactotransferrin has antimicrobial activity. The most effective inhibitory activity was seen against E.coli and P.aeruginosa.<ref>PMID:8980754</ref> <ref>PMID:15222473</ref> Lactoferricin B is an antimicrobial peptide. Inhibits the growth of Gram-negative and Gram-positive bacteria.<ref>PMID:8980754</ref> <ref>PMID:15222473</ref> The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions. This function contributes to the antimicrobial activity.<ref>PMID:8980754</ref> <ref>PMID:15222473</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The bilobal lactoferrin is an approximately 76 kDa glycoprotein. It sequesters two Fe(3+) ions together with two CO32- ions. The C-terminal half (residues, Tyr342-Arg689, C-lobe) of bovine lactoferrin (BLF) (residues Ala1-Arg689) was prepared by limited proteolysis using trypsin. Both C-lobe and intact BLF were saturated to 100%. Both of them retained up to nearly 85% of iron at pH 6.5. At pH 5.0, C-lobe retained 75% of iron whereas intact protein could retain only slightly more than 60%. At pH 4.0 both contained 25% iron and at pH 2.0 they were left with iron concentration of only 10%. The structure of iron saturated C-lobe was determined at 2.79 A resolution and refined to Rcryst and Rfree factors of 0.205 and 0.273, respectively. The structure contains two crystallographically independent molecules, A and B. They were found to have identical structures with an r.m.s. shift of 0.5 A for their C(alpha) atoms. A high solvent content of 66% was observed in the crystals. The average value of an overall B-factor was 68.0 A(2) . The distance of 2.9 A observed for the coordination bond between Fe(3+) ion and N(e2) of His595 appeared to be considerably longer than the normally observed values of 1.9-2.2 A. This indicated that the coordination bond involving His595 may be absent. Other coordination distances were observed in the range of 2.1-2.3 A. Based on the present structure of iron saturated C-lobe, it may be stated that His595 is the first residue to dissociate from ferric ion when the pH is lowered. Proteins 2016; 84:591-599. (c) 2016 Wiley Periodicals, Inc. | ||
| - | + | Structure of iron saturated C-lobe of bovine lactoferrin at pH 6.8 indicates a weakening of iron coordination.,Rastogi N, Singh A, Singh PK, Tyagi TK, Pandey S, Shin K, Kaur P, Sharma S, Singh TP Proteins. 2016 May;84(5):591-9. doi: 10.1002/prot.25004. Epub 2016 Feb 24. PMID:26850578<ref>PMID:26850578</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5hbc" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | |
| - | [[Category: Rastogi | + | ==See Also== |
| - | [[Category: Singh | + | *[[Lactoferrin|Lactoferrin]] |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Bos taurus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Kaur P]] | ||
| + | [[Category: Rastogi N]] | ||
| + | [[Category: Sharma S]] | ||
| + | [[Category: Singh A]] | ||
| + | [[Category: Singh PK]] | ||
| + | [[Category: Singh TP]] | ||
| + | [[Category: Tyagi TK]] | ||
Current revision
Intermediate structure of iron-saturated C-lobe of bovine lactoferrin at 2.79 Angstrom resolution indicates the softening of iron coordination
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Categories: Bos taurus | Large Structures | Kaur P | Rastogi N | Sharma S | Singh A | Singh PK | Singh TP | Tyagi TK
