1a4v

From Proteopedia

(Difference between revisions)

Current revision

ALPHA-LACTALBUMIN

Structural highlights

1a4v is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.8Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LALBA_HUMAN 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 high-resolution X-ray crystal structure of human alpha-lactalbumin (at 1.8 A) in the presence of an elevated level of calcium reveals a new secondary calcium binding site, 7.9 A away from the primary calcium binding site known in all alpha-lactalbumin structures so far. The new calcium binding site is different from the zinc and sulfate binding sites [Ren, J., et al. (1993) J. Biol. Chem. 268, 19292-19298] but shares common features with the manganese binding site as described by Gerkin [Gerkin, T. A. (1984) Biochemistry 23, 4688-4697]. The proximity of the manganese and calcium binding region and the location of the functional site on one side of the charged surface of the alpha-lactalbumin molecule suggest that these binding sites might play a role in the formation of the lactose synthase complex.

Structural evidence for the presence of a secondary calcium binding site in human alpha-lactalbumin.,Chandra N, Brew K, Acharya KR Biochemistry. 1998 Apr 7;37(14):4767-72. PMID:9537992^[1]

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

References

↑ Chandra N, Brew K, Acharya KR. Structural evidence for the presence of a secondary calcium binding site in human alpha-lactalbumin. Biochemistry. 1998 Apr 7;37(14):4767-72. PMID:9537992 doi:http://dx.doi.org/10.1021/bi973000t

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://proteopedia.org/wiki/index.php/1a4v"

Categories: Homo sapiens | Large Structures | Acharya KR | Chandra N

@@ Line 1: / Line 1: @@
-[[Image:1a4v.gif|left|200px]]<br />
-<applet load="1a4v" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1a4v, resolution 1.8&Aring;" />
-'''ALPHA-LACTALBUMIN'''<br />
-==Overview==
+==ALPHA-LACTALBUMIN==
-The high-resolution X-ray crystal structure of human alpha-lactalbumin (at, 1.8 A) in the presence of an elevated level of calcium reveals a new, secondary calcium binding site, 7.9 A away from the primary calcium, binding site known in all alpha-lactalbumin structures so far. The new, calcium binding site is different from the zinc and sulfate binding sites, [Ren, J., et al. (1993) J. Biol. Chem. 268, 19292-19298] but shares common, features with the manganese binding site as described by Gerkin [Gerkin, T. A. (1984) Biochemistry 23, 4688-4697]. The proximity of the manganese, and calcium binding region and the location of the functional site on one, side of the charged surface of the alpha-lactalbumin molecule suggest that, these binding sites might play a role in the formation of the lactose, synthase complex.
+<StructureSection load='1a4v' size='340' side='right'caption='[[1a4v]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1a4v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A4V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A4V 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]] 1.8&#8491;</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a4v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a4v OCA], [https://pdbe.org/1a4v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a4v RCSB], [https://www.ebi.ac.uk/pdbsum/1a4v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a4v ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/LALBA_HUMAN LALBA_HUMAN] 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 ==
+[[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/a4/1a4v_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=1a4v ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The high-resolution X-ray crystal structure of human alpha-lactalbumin (at 1.8 A) in the presence of an elevated level of calcium reveals a new secondary calcium binding site, 7.9 A away from the primary calcium binding site known in all alpha-lactalbumin structures so far. The new calcium binding site is different from the zinc and sulfate binding sites [Ren, J., et al. (1993) J. Biol. Chem. 268, 19292-19298] but shares common features with the manganese binding site as described by Gerkin [Gerkin, T. A. (1984) Biochemistry 23, 4688-4697]. The proximity of the manganese and calcium binding region and the location of the functional site on one side of the charged surface of the alpha-lactalbumin molecule suggest that these binding sites might play a role in the formation of the lactose synthase complex.
-==About this Structure==
+Structural evidence for the presence of a secondary calcium binding site in human alpha-lactalbumin.,Chandra N, Brew K, Acharya KR Biochemistry. 1998 Apr 7;37(14):4767-72. PMID:9537992<ref>PMID:9537992</ref>
-A4V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Structure known Active Sites: CB1 and CB2. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A4V OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Structural evidence for the presence of a secondary calcium binding site in human alpha-lactalbumin., Chandra N, Brew K, Acharya KR, Biochemistry. 1998 Apr 7;37(14):4767-72. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9537992 9537992]
+</div>
-[[Category: Homo sapiens]]
+<div class="pdbe-citations 1a4v" style="background-color:#fffaf0;"></div>
-[[Category: Lactose synthase]]
-[[Category: Single protein]]
-[[Category: Acharya, K.R.]]
-[[Category: Chandra, N.]]
-[[Category: CA]]
-[[Category: alpha-lactalbumin]]
-[[Category: calcium binding]]
-[[Category: lactose synthase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 15:55:41 2007''
+==See Also==
+*[[Alpha-lactalbumin 3D structures|Alpha-lactalbumin 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Acharya KR]]
+[[Category: Chandra N]]

1a4v

From Proteopedia

Current revision

ALPHA-LACTALBUMIN

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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