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.

1fkq

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 10:26, 18 November 2020

RECOMBINANT GOAT ALPHA-LACTALBUMIN T29V

Structural highlights

1fkq is a 1 chain structure with sequence from African dwarf goat. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1hmk, 1hfy, 1fkv
Gene:	A CLONED GENE OF GOAT LACTA (African dwarf goat)
Activity:	Lactose synthase, with EC number 2.4.1.22
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.

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^[1]

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

References

↑ Horii K, Saito M, Yoda T, Tsumoto K, Matsushima M, Kuwajima K, Kumagai I. Contribution of Thr29 to the thermodynamic stability of goat alpha-lactalbumin as determined by experimental and theoretical approaches. Proteins. 2001 Oct 1;45(1):16-29. PMID:11536356

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/1fkq"

@@ Line 1: / Line 1: @@
 ==RECOMBINANT GOAT ALPHA-LACTALBUMIN T29V==
-<StructureSection load='1fkq' size='340' side='right' caption='[[1fkq]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+<StructureSection load='1fkq' size='340' side='right'caption='[[1fkq]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1fkq]] is a 1 chain structure with sequence from [http://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=1FKQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FKQ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1fkq]] is a 1 chain structure with sequence from [http://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=1FKQ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1FKQ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
+</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hmk|1hmk]], [[1hfy|1hfy]], [[1fkv|1fkv]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">A CLONED GENE OF GOAT LACTA ([http://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'>[http://en.wikipedia.org/wiki/Lactose_synthase Lactose synthase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fkq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fkq OCA], [http://pdbe.org/1fkq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fkq RCSB], [http://www.ebi.ac.uk/pdbsum/1fkq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fkq ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1fkq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fkq OCA], [http://pdbe.org/1fkq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fkq RCSB], [http://www.ebi.ac.uk/pdbsum/1fkq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fkq ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 31: / Line 31: @@
 </div>
 <div class="pdbe-citations 1fkq" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Alpha-lactalbumin 3D structures|Alpha-lactalbumin 3D structures]]
 == References ==
 <references/>
@@ Line 37: / Line 40: @@
 [[Category: African dwarf goat]]
 [[Category: Lactose synthase]]
+[[Category: Large Structures]]
 [[Category: Horii, K]]
 [[Category: Kumagai, I]]

1fkq

From Proteopedia

Revision as of 10:26, 18 November 2020

RECOMBINANT GOAT ALPHA-LACTALBUMIN T29V

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox