This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1biy

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (15:33, 13 March 2024) (edit) (undo)
 
(21 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1biy.gif|left|200px]]<br />
 
-
<applet load="1biy" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1biy, resolution 3.37&Aring;" />
 
-
'''STRUCTURE OF DIFERRIC BUFFALO LACTOFERRIN'''<br />
 
-
==Overview==
+
==STRUCTURE OF DIFERRIC BUFFALO LACTOFERRIN==
-
The three-dimensional structure of diferric buffalo lactoferrin has been, determined at 3.3 A resolution. The structure was solved by molecular, replacement using the coordinates of diferric human lactoferrin as a, search model and was refined by simulated annealing (X-PLOR). The final, model comprises 5316 protein atoms for all 689 residues, two Fe(3+) and, two CO(3)(2-) ions. The final R factor was 21.8% for 11 711 reflections in, the resolution range 17.0-3.3 A. The folding of buffalo lactoferrin is, essentially similar to that of the other members of the transferrin, family. The significant differences are found in the dimensions of the, binding cleft and the interlobe orientation. The interlobe interactions, are predominantly hydrophobic in nature, thus facilitating the sliding of, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?10818344 (full description)]]
+
<StructureSection load='1biy' size='340' side='right'caption='[[1biy]], [[Resolution|resolution]] 3.37&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1biy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bubalus_bubalis Bubalus bubalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BIY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BIY 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]] 3.37&#8491;</td></tr>
 +
<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></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=1biy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1biy OCA], [https://pdbe.org/1biy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1biy RCSB], [https://www.ebi.ac.uk/pdbsum/1biy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1biy ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/TRFL_BUBBU TRFL_BUBBU] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. 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 (By similarity).
 +
== 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/bi/1biy_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1biy ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1BIY is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bubalus_bubalis Bubalus bubalis]] with FE and CO3 as [[http://en.wikipedia.org/wiki/ligands ligands]]. Structure known Active Sites: FE1 and FE2. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BIY OCA]].
+
*[[Lactoferrin|Lactoferrin]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
Structure of buffalo lactoferrin at 3.3 A resolution at 277 K., Karthikeyan S, Yadav S, Paramasivam M, Srinivasan A, Singh TP, Acta Crystallogr D Biol Crystallogr. 2000 Jun;56(Pt 6):684-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10818344 10818344]
+
[[Category: Bubalus bubalis]]
[[Category: Bubalus bubalis]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Karthikeyan, S.]]
+
[[Category: Karthikeyan S]]
-
[[Category: Singh, T.P.]]
+
[[Category: Singh TP]]
-
[[Category: Yadav, S.]]
+
[[Category: Yadav S]]
-
[[Category: CO3]]
+
-
[[Category: FE]]
+
-
[[Category: antibacterial]]
+
-
[[Category: iron binding protein]]
+
-
[[Category: lactoferrin]]
+
-
[[Category: structure]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:55:14 2007''
+

Current revision

STRUCTURE OF DIFERRIC BUFFALO LACTOFERRIN

PDB ID 1biy

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools