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- | [[Image:3ci8.jpg|left|200px]] | |
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- | {{Structure
| + | ==Crystal structure of the complex of C-lobe of lactoferrin with vitamin B3 (niacin) at 2.4 A resolution== |
- | |PDB= 3ci8 |SIZE=350|CAPTION= <scene name='initialview01'>3ci8</scene>, resolution 2.4Å
| + | <StructureSection load='3ci8' size='340' side='right'caption='[[3ci8]], [[Resolution|resolution]] 2.40Å' scene=''> |
- | |SITE= <scene name='pdbsite=AC1:Nag+Binding+Site+For+Residue+A+1'>AC1</scene>, <scene name='pdbsite=AC2:Nag+Binding+Site+For+Residue+A+2'>AC2</scene>, <scene name='pdbsite=AC3:Nag+Binding+Site+For+Residue+A+3'>AC3</scene>, <scene name='pdbsite=AC4:Nag+Binding+Site+For+Residue+A+4'>AC4</scene>, <scene name='pdbsite=AC5:Nag+Binding+Site+For+Residue+A+5'>AC5</scene>, <scene name='pdbsite=AC6:Fe+Binding+Site+For+Residue+A+6'>AC6</scene>, <scene name='pdbsite=AC7:Co3+Binding+Site+For+Residue+A+7'>AC7</scene>, <scene name='pdbsite=AC8:Zn+Binding+Site+For+Residue+A+8'>AC8</scene>, <scene name='pdbsite=AC9:Zn+Binding+Site+For+Residue+A+9'>AC9</scene>, <scene name='pdbsite=BC1:So4+Binding+Site+For+Residue+A+10'>BC1</scene> and <scene name='pdbsite=BC2:Nio+Binding+Site+For+Residue+A+11'>BC2</scene>
| + | == Structural highlights == |
- | |LIGAND= <scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NIO:NICOTINIC+ACID'>NIO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
| + | <table><tr><td colspan='2'>[[3ci8]] is a 1 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=3CI8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CI8 FirstGlance]. <br> |
- | |ACTIVITY=
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> |
- | |GENE=
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NIO:NICOTINIC+ACID'>NIO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
- | |DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=smart00094 TR_FER]</span>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ci8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ci8 OCA], [https://pdbe.org/3ci8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ci8 RCSB], [https://www.ebi.ac.uk/pdbsum/3ci8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ci8 ProSAT]</span></td></tr> |
- | |RELATEDENTRY=[[2dyx|2dyx]], [[2r9j|2r9j]], [[2px1|2px1]], [[2qz1|2qz1]]
| + | </table> |
- | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ci8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ci8 OCA], [http://www.ebi.ac.uk/pdbsum/3ci8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3ci8 RCSB]</span>
| + | == 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> |
| + | == 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/ci/3ci8_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=3ci8 ConSurf]. |
| + | <div style="clear:both"></div> |
| | | |
- | '''Crystal structure of the complex of C-lobe of lactoferrin with vitamin B3 (niacin) at 2.4 A resolution'''
| + | ==See Also== |
- | | + | *[[Lactoferrin|Lactoferrin]] |
- | | + | == References == |
- | ==About this Structure== | + | <references/> |
- | 3CI8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CI8 OCA].
| + | __TOC__ |
| + | </StructureSection> |
| [[Category: Bos taurus]] | | [[Category: Bos taurus]] |
- | [[Category: Single protein]] | + | [[Category: Large Structures]] |
- | [[Category: Kaur, P.]] | + | [[Category: Kaur P]] |
- | [[Category: Kushwaha, G S.]] | + | [[Category: Kushwaha GS]] |
- | [[Category: Sharma, S.]] | + | [[Category: Sharma S]] |
- | [[Category: Singh, N.]] | + | [[Category: Singh N]] |
- | [[Category: Singh, T P.]] | + | [[Category: Singh TP]] |
- | [[Category: Vikram, G.]] | + | [[Category: Vikram G]] |
- | [[Category: antibiotic]]
| + | |
- | [[Category: antimicrobial]]
| + | |
- | [[Category: c-lobe]]
| + | |
- | [[Category: complex]]
| + | |
- | [[Category: crystal structure]]
| + | |
- | [[Category: glycoprotein]]
| + | |
- | [[Category: hydrolase]]
| + | |
- | [[Category: ion transport]]
| + | |
- | [[Category: iron]]
| + | |
- | [[Category: iron transport]]
| + | |
- | [[Category: metal binding protein]]
| + | |
- | [[Category: metal-binding]]
| + | |
- | [[Category: niacin]]
| + | |
- | [[Category: protease]]
| + | |
- | [[Category: secreted]]
| + | |
- | [[Category: serine protease]]
| + | |
- | [[Category: transport]]
| + | |
- | [[Category: vitamin b3]]
| + | |
- | | + | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:32:22 2008''
| + | |
| Structural highlights
3ci8 is a 1 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| Method: | X-ray diffraction, Resolution 2.4Å |
Ligands: | , , , , , |
Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
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.[1] [2] Lactotransferrin has antimicrobial activity. The most effective inhibitory activity was seen against E.coli and P.aeruginosa.[3] [4] Lactoferricin B is an antimicrobial peptide. Inhibits the growth of Gram-negative and Gram-positive bacteria.[5] [6] 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.[7] [8]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
See Also
References
- ↑ Hoek KS, Milne JM, Grieve PA, Dionysius DA, Smith R. Antibacterial activity in bovine lactoferrin-derived peptides. Antimicrob Agents Chemother. 1997 Jan;41(1):54-9. PMID:8980754
- ↑ Massucci MT, Giansanti F, Di Nino G, Turacchio M, Giardi MF, Botti D, Ippoliti R, De Giulio B, Siciliano RA, Donnarumma G, Valenti P, Bocedi A, Polticelli F, Ascenzi P, Antonini G. Proteolytic activity of bovine lactoferrin. Biometals. 2004 Jun;17(3):249-55. PMID:15222473
- ↑ Hoek KS, Milne JM, Grieve PA, Dionysius DA, Smith R. Antibacterial activity in bovine lactoferrin-derived peptides. Antimicrob Agents Chemother. 1997 Jan;41(1):54-9. PMID:8980754
- ↑ Massucci MT, Giansanti F, Di Nino G, Turacchio M, Giardi MF, Botti D, Ippoliti R, De Giulio B, Siciliano RA, Donnarumma G, Valenti P, Bocedi A, Polticelli F, Ascenzi P, Antonini G. Proteolytic activity of bovine lactoferrin. Biometals. 2004 Jun;17(3):249-55. PMID:15222473
- ↑ Hoek KS, Milne JM, Grieve PA, Dionysius DA, Smith R. Antibacterial activity in bovine lactoferrin-derived peptides. Antimicrob Agents Chemother. 1997 Jan;41(1):54-9. PMID:8980754
- ↑ Massucci MT, Giansanti F, Di Nino G, Turacchio M, Giardi MF, Botti D, Ippoliti R, De Giulio B, Siciliano RA, Donnarumma G, Valenti P, Bocedi A, Polticelli F, Ascenzi P, Antonini G. Proteolytic activity of bovine lactoferrin. Biometals. 2004 Jun;17(3):249-55. PMID:15222473
- ↑ Hoek KS, Milne JM, Grieve PA, Dionysius DA, Smith R. Antibacterial activity in bovine lactoferrin-derived peptides. Antimicrob Agents Chemother. 1997 Jan;41(1):54-9. PMID:8980754
- ↑ Massucci MT, Giansanti F, Di Nino G, Turacchio M, Giardi MF, Botti D, Ippoliti R, De Giulio B, Siciliano RA, Donnarumma G, Valenti P, Bocedi A, Polticelli F, Ascenzi P, Antonini G. Proteolytic activity of bovine lactoferrin. Biometals. 2004 Jun;17(3):249-55. PMID:15222473
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