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1b7u

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Revision as of 06:57, 24 February 2021

Structure of Mare Apolactoferrin: the N and C Lobes are in the Closed Form

Structural highlights

1b7u is a 1 chain structure with sequence from Equus caballus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TRFL_HORSE] 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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The structure of mare apolactoferrin (MALT) has been determined at 3. 8 A resolution by the molecular-replacement method, using the structure of mare diferric lactoferrin (MDLT) as the search model. The MDLT structure contains two iron-binding sites: one in the N-terminal lobe, lying between domains N1 and N2, and one in the C-terminal lobe between domains C1 and C2. Both lobes have a closed structure. MALT was crystallized using the microdialysis method with 10%(v/v) ethanol in 0.01 M Tris-HCl. The structure has been refined to a final R factor of 0.20 for all data to 3.8 A resolution. Comparison of the structure of MALT with that of MDLT showed that the domain arrangements in these structures are identical. However, the structure of MALT is very different to the structures of human apolactoferrin (HALT) and duck apo-ovotransferrin (DAOT), in which the domain associations differ greatly. In HALT, the N lobe adopts an open conformation while the C lobe is in the closed form. On the other hand, in DAOT both the N and the C lobes adopt the open form. These results indicate the domain arrangements in these proteins to be an important structural feature related to their specific biological functions. Based on the structures of MALT, HALT and DAOT, it can be stated that the native apoproteins of the transferrin family adopt three forms: (i) with both the N and the C lobes in closed forms, as observed in MALT, (ii) with the N lobe open and the C lobe closed, as observed in HALT, and (iii) with both the N and the C lobes open, as found in DAOT. All these proteins attain a convergent form when iron is bound to them, suggesting an efficient and unique form of iron binding. The interface between the N and C lobes, which is formed by N1-C1 contact in the core of the molecule, does not change significantly.

Structure of mare apolactoferrin: the N and C lobes are in the closed form.,Sharma AK, Rajashankar KR, Yadav MP, Singh TP Acta Crystallogr D Biol Crystallogr. 1999 Jun;55(Pt 6):1152-7. PMID:10329777^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Sharma AK, Rajashankar KR, Yadav MP, Singh TP. Structure of mare apolactoferrin: the N and C lobes are in the closed form. Acta Crystallogr D Biol Crystallogr. 1999 Jun;55(Pt 6):1152-7. PMID:10329777

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1b7u"

@@ Line 3: / Line 3: @@
 <StructureSection load='1b7u' size='340' side='right'caption='[[1b7u]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1b7u]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B7U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1B7U FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1b7u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B7U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B7U FirstGlance]. <br>
-</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=1b7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b7u OCA], [http://pdbe.org/1b7u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1b7u RCSB], [http://www.ebi.ac.uk/pdbsum/1b7u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1b7u ProSAT]</span></td></tr>
+</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=1b7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b7u OCA], [https://pdbe.org/1b7u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b7u RCSB], [https://www.ebi.ac.uk/pdbsum/1b7u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b7u ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/TRFL_HORSE TRFL_HORSE]] 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).
+[[https://www.uniprot.org/uniprot/TRFL_HORSE TRFL_HORSE]] 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]]

1b7u

From Proteopedia

Revision as of 06:57, 24 February 2021

Structure of Mare Apolactoferrin: the N and C Lobes are in the Closed Form

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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