1hml

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(New page: 200px<br /> <applet load="1hml" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hml, resolution 1.7&Aring;" /> '''ALPHA_LACTALBUMIN PO...)
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[[Image:1hml.gif|left|200px]]<br /><applet load="1hml" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1hml" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1hml, resolution 1.7&Aring;" />
caption="1hml, resolution 1.7&Aring;" />
'''ALPHA_LACTALBUMIN POSSESSES A DISTINCT ZINC BINDING SITE'''<br />
'''ALPHA_LACTALBUMIN POSSESSES A DISTINCT ZINC BINDING SITE'''<br />
==Overview==
==Overview==
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It has been proposed that the binding of Zn2+ to alpha-lactalbumin, switches the conformation to one akin to a state intermediate in the, folding of the protein. However, the high resolution x-ray crystal, structure of human alpha-lactalbumin-Zn2+ complex at 1.7-A resolution (pH, 7.6) does not reveal any significant change in conformation from the, native state. The Zn2+ ion binds specifically in the "cleft" of, alpha-lactalbumin (the region which forms the active site of the, homologous protein lysozyme). This may suggest a possible role for Zn2+, binding in lactose synthase complex. The coordination of the Zn2+ ion, involves a symmetry-related molecule in the crystal, the crystal contacts, being stabilized by a SO4(2-) ion bound at the interface between three, molecules.
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It has been proposed that the binding of Zn2+ to alpha-lactalbumin switches the conformation to one akin to a state intermediate in the folding of the protein. However, the high resolution x-ray crystal structure of human alpha-lactalbumin-Zn2+ complex at 1.7-A resolution (pH 7.6) does not reveal any significant change in conformation from the native state. The Zn2+ ion binds specifically in the "cleft" of alpha-lactalbumin (the region which forms the active site of the homologous protein lysozyme). This may suggest a possible role for Zn2+ binding in lactose synthase complex. The coordination of the Zn2+ ion involves a symmetry-related molecule in the crystal, the crystal contacts being stabilized by a SO4(2-) ion bound at the interface between three molecules.
==About this Structure==
==About this Structure==
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1HML 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, ZN and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. 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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HML OCA].
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1HML 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 <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HML OCA].
==Reference==
==Reference==
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[[Category: Lactose synthase]]
[[Category: Lactose synthase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Acharya, K.R.]]
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[[Category: Acharya, K R.]]
[[Category: Ren, J.]]
[[Category: Ren, J.]]
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[[Category: Stuart, D.I.]]
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[[Category: Stuart, D I.]]
[[Category: CA]]
[[Category: CA]]
[[Category: SO4]]
[[Category: SO4]]
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[[Category: calcium-binding protein]]
[[Category: calcium-binding protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:20:12 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:02:48 2008''

Revision as of 11:02, 21 February 2008


1hml, resolution 1.7Å

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ALPHA_LACTALBUMIN POSSESSES A DISTINCT ZINC BINDING SITE

Overview

It has been proposed that the binding of Zn2+ to alpha-lactalbumin switches the conformation to one akin to a state intermediate in the folding of the protein. However, the high resolution x-ray crystal structure of human alpha-lactalbumin-Zn2+ complex at 1.7-A resolution (pH 7.6) does not reveal any significant change in conformation from the native state. The Zn2+ ion binds specifically in the "cleft" of alpha-lactalbumin (the region which forms the active site of the homologous protein lysozyme). This may suggest a possible role for Zn2+ binding in lactose synthase complex. The coordination of the Zn2+ ion involves a symmetry-related molecule in the crystal, the crystal contacts being stabilized by a SO4(2-) ion bound at the interface between three molecules.

About this Structure

1HML is a Single protein structure of sequence from Homo sapiens with , and as ligands. Active as Lactose synthase, with EC number 2.4.1.22 Full crystallographic information is available from OCA.

Reference

Alpha-lactalbumin possesses a distinct zinc binding site., Ren J, Stuart DI, Acharya KR, J Biol Chem. 1993 Sep 15;268(26):19292-8. PMID:8366079

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