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[[Image:3cfl.jpg|left|200px]]


{{Structure
==Crystal structure of the complex formed between C-lobe of bovine lactoferrin and 5-chloro-6'-methyl-3-[4-(methylsulfonyl)phenyl]-2,3'-bipyridine at 2.25 A resolution==
|PDB= 3cfl |SIZE=350|CAPTION= <scene name='initialview01'>3cfl</scene>, resolution 2.25&Aring;
<StructureSection load='3cfl' size='340' side='right'caption='[[3cfl]], [[Resolution|resolution]] 2.25&Aring;' 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+687'>AC3</scene>, <scene name='pdbsite=AC4:Nag+Binding+Site+For+Residue+A+688'>AC4</scene>, <scene name='pdbsite=AC5:Nag+Binding+Site+For+Residue+A+689'>AC5</scene>, <scene name='pdbsite=AC6:Nag+Binding+Site+For+Residue+A+690'>AC6</scene>, <scene name='pdbsite=AC7:Fe+Binding+Site+For+Residue+A+691'>AC7</scene>, <scene name='pdbsite=AC8:Co3+Binding+Site+For+Residue+A+692'>AC8</scene>, <scene name='pdbsite=AC9:Zn+Binding+Site+For+Residue+A+3'>AC9</scene>, <scene name='pdbsite=BC1:Zn+Binding+Site+For+Residue+A+4'>BC1</scene>, <scene name='pdbsite=BC2:So4+Binding+Site+For+Residue+A+5'>BC2</scene> and <scene name='pdbsite=BC3:5ch+Binding+Site+For+Residue+A+693'>BC3</scene>
== Structural highlights ==
|LIGAND= <scene name='pdbligand=5CH:5-CHLORO-6&#39;-METHYL-3-[4-(METHYLSULFONYL)PHENYL]-2,3&#39;-BIPYRIDINE'>5CH</scene>, <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=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
<table><tr><td colspan='2'>[[3cfl]] 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=3CFL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CFL 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]] 2.25&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5CH:5-CHLORO-6-METHYL-3-[4-(METHYLSULFONYL)PHENYL]-2,3-BIPYRIDINE'>5CH</scene>, <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=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3cfl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cfl OCA], [https://pdbe.org/3cfl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cfl RCSB], [https://www.ebi.ac.uk/pdbsum/3cfl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cfl 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=3cfl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cfl OCA], [http://www.ebi.ac.uk/pdbsum/3cfl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3cfl 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/cf/3cfl_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=3cfl ConSurf].
<div style="clear:both"></div>


'''Crystal structure of the complex formed between C-lobe of bovine lactoferrin and 5-chloro-6'-methyl-3-[4-(methylsulfonyl)phenyl]-2,3'-bipyridine at 2.25 A resolution'''
==See Also==
 
*[[Lactoferrin|Lactoferrin]]
 
== References ==
==About this Structure==
<references/>
3CFL 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=3CFL OCA].
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Kaur, P.]]
[[Category: Kaur P]]
[[Category: Mir, R.]]
[[Category: Mir R]]
[[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: etoricoxib]]
[[Category: glycoprotein]]
[[Category: hydrolase]]
[[Category: ion transport]]
[[Category: iron]]
[[Category: iron transport]]
[[Category: metal binding protein]]
[[Category: metal-binding]]
[[Category: protease]]
[[Category: secreted]]
[[Category: serine protease]]
[[Category: transport]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:32:06 2008''

Latest revision as of 04:40, 21 November 2024

Crystal structure of the complex formed between C-lobe of bovine lactoferrin and 5-chloro-6'-methyl-3-[4-(methylsulfonyl)phenyl]-2,3'-bipyridine at 2.25 A resolutionCrystal structure of the complex formed between C-lobe of bovine lactoferrin and 5-chloro-6'-methyl-3-[4-(methylsulfonyl)phenyl]-2,3'-bipyridine at 2.25 A resolution

Structural highlights

3cfl 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 2.25Å
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

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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
  5. ↑ 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
  6. ↑ 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
  7. ↑ 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
  8. ↑ 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

3cfl, resolution 2.25Å

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