1fkv: Difference between revisions

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<StructureSection load='1fkv' size='340' side='right'caption='[[1fkv]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1fkv' size='340' side='right'caption='[[1fkv]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1fkv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/African_dwarf_goat African dwarf goat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FKV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FKV FirstGlance]. <br>
<table><tr><td colspan='2'>[[1fkv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Capra_hircus Capra hircus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FKV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FKV FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
</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&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1hmk|1hmk]], [[1fkq|1fkq]], [[1hfy|1hfy]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">A CLONED GENE OF GOAT LACTA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9925 African dwarf goat])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Lactose_synthase Lactose synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.22 2.4.1.22] </span></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=1fkv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fkv OCA], [https://pdbe.org/1fkv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fkv RCSB], [https://www.ebi.ac.uk/pdbsum/1fkv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fkv ProSAT]</span></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=1fkv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fkv OCA], [https://pdbe.org/1fkv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fkv RCSB], [https://www.ebi.ac.uk/pdbsum/1fkv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fkv ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/LALBA_CAPHI LALBA_CAPHI]] Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose onto the N-acetylglucosamine of the oligosaccharide chains in glycoproteins.  
[https://www.uniprot.org/uniprot/LALBA_CAPHI LALBA_CAPHI] Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose onto the N-acetylglucosamine of the oligosaccharide chains in glycoproteins.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1fkv ConSurf].
</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=1fkv ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Thr29 residue in the hydrophobic core of goat alpha-lactalbumin (alpha-LA) was substituted with Val (Thr29Val) and Ile (Thr29Ile) to investigate the contribution of Thr29 to the thermodynamic stability of the protein. We carried out protein stability measurements, X-ray crystallographic analyses, and free energy calculations based on molecular dynamics simulation. The equilibrium unfolding transitions induced by guanidine hydrochloride demonstrated that the Thr29Val and Thr29Ile mutants were, respectively, 1.9 and 3.2 kcal/mol more stable than the wild-type protein (WT). The overall structures of the mutants were almost identical to that of WT, in spite of the disruption of the hydrogen bonding between the side-chain O-H group of Thr29 and the main-chain C=O group of Glu25. To analyze the stabilization mechanism of the mutants, we performed free energy calculations. The calculated free energy differences were in good agreement with the experimental values. The stabilization of the mutants was mainly caused by solvation loss in the denatured state. Furthermore, the O-H group of Thr29 favorably interacts with the C=O group of Glu25 to form hydrogen bonds and, simultaneously, unfavorably interacts electrostatically with the main-chain C=O group of Thr29. The difference in the free energy profile of the unfolding path between WT and the Thr29Ile mutant is discussed in light of our experimental and theoretical results.
Contribution of Thr29 to the thermodynamic stability of goat alpha-lactalbumin as determined by experimental and theoretical approaches.,Horii K, Saito M, Yoda T, Tsumoto K, Matsushima M, Kuwajima K, Kumagai I Proteins. 2001 Oct 1;45(1):16-29. PMID:11536356<ref>PMID:11536356</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1fkv" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Alpha-lactalbumin 3D structures|Alpha-lactalbumin 3D structures]]
*[[Alpha-lactalbumin 3D structures|Alpha-lactalbumin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: African dwarf goat]]
[[Category: Capra hircus]]
[[Category: Lactose synthase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Horii, K]]
[[Category: Horii K]]
[[Category: Kumagai, I]]
[[Category: Kumagai I]]
[[Category: Matsushima, M]]
[[Category: Matsushima M]]
[[Category: Tsumoto, K]]
[[Category: Tsumoto K]]
[[Category: Calcium binding metalloprotein]]
[[Category: Glycoprotein]]
[[Category: Lactose synthase component]]
[[Category: Transferase]]

Revision as of 14:13, 27 March 2024

RECOMBINANT GOAT ALPHA-LACTALBUMIN T29IRECOMBINANT GOAT ALPHA-LACTALBUMIN T29I

Structural highlights

1fkv is a 1 chain structure with sequence from Capra hircus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LALBA_CAPHI Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose onto the N-acetylglucosamine of the oligosaccharide chains in glycoproteins.

Evolutionary Conservation

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

See Also

1fkv, resolution 2.00Å

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