1v0j

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[[Image:1v0j.gif|left|200px]]<br /><applet load="1v0j" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1v0j.gif|left|200px]]
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caption="1v0j, resolution 2.25&Aring;" />
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'''UDP-GALACTOPYRANOSE MUTASE FROM MYCOBACTERIUM TUBERCULOSIS'''<br />
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{{Structure
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|PDB= 1v0j |SIZE=350|CAPTION= <scene name='initialview01'>1v0j</scene>, resolution 2.25&Aring;
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|SITE= <scene name='pdbsite=AC1:Fad+Binding+Site+For+Chain+D'>AC1</scene>
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|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> and <scene name='pdbligand=BCN:BICINE'>BCN</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/UDP-galactopyranose_mutase UDP-galactopyranose mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.9 5.4.99.9]
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|GENE=
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}}
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'''UDP-GALACTOPYRANOSE MUTASE FROM MYCOBACTERIUM TUBERCULOSIS'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1V0J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with <scene name='pdbligand=FAD:'>FAD</scene> and <scene name='pdbligand=BCN:'>BCN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/UDP-galactopyranose_mutase UDP-galactopyranose mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.9 5.4.99.9] Known structural/functional Site: <scene name='pdbsite=AC1:Fad+Binding+Site+For+Chain+D'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V0J OCA].
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1V0J is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V0J OCA].
==Reference==
==Reference==
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Crystal structures of Mycobacteria tuberculosis and Klebsiella pneumoniae UDP-galactopyranose mutase in the oxidised state and Klebsiella pneumoniae UDP-galactopyranose mutase in the (active) reduced state., Beis K, Srikannathasan V, Liu H, Fullerton SW, Bamford VA, Sanders DA, Whitfield C, McNeil MR, Naismith JH, J Mol Biol. 2005 May 13;348(4):971-82. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15843027 15843027]
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Crystal structures of Mycobacteria tuberculosis and Klebsiella pneumoniae UDP-galactopyranose mutase in the oxidised state and Klebsiella pneumoniae UDP-galactopyranose mutase in the (active) reduced state., Beis K, Srikannathasan V, Liu H, Fullerton SW, Bamford VA, Sanders DA, Whitfield C, McNeil MR, Naismith JH, J Mol Biol. 2005 May 13;348(4):971-82. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15843027 15843027]
[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: mutase]]
[[Category: mutase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:30:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:39:16 2008''

Revision as of 12:39, 20 March 2008


PDB ID 1v0j

Drag the structure with the mouse to rotate
, resolution 2.25Å
Sites:
Ligands: and
Activity: UDP-galactopyranose mutase, with EC number 5.4.99.9
Coordinates: save as pdb, mmCIF, xml



UDP-GALACTOPYRANOSE MUTASE FROM MYCOBACTERIUM TUBERCULOSIS


Overview

Uridine diphosphogalactofuranose (UDP-Galf) is the precursor of the d-galactofuranose sugar found in bacterial and parasitic cell walls, including those of many pathogens. UDP-Galf is made from UDP-galactopyranose by the enzyme UDP-galactopyranose mutase. The enzyme requires the reduced FADH- co-factor for activity. The structure of the Mycobacterium tuberculosis mutase with FAD has been determined to 2.25 A. The structures of Klebsiella pneumoniae mutase with FAD and with FADH- bound have been determined to 2.2 A and 2.35 A resolution, respectively. This is the first report of the FADH(-)-containing structure. Two flavin-dependent mechanisms for the enzyme have been proposed, one, which involves a covalent adduct being formed at the flavin and the other based on electron transfer. Using our structural data, we have examined the two mechanisms. The electron transfer mechanism is consistent with the structural data, not surprisingly, since it makes fewer demands on the precise positioning of atoms. A model based on a covalent adduct FAD requires repositioning of the enzyme active site and would appear to require the isoalloxazine ring of FADH- to buckle in a particular way. However, the FADH- structure reveals that the isoalloxazine ring buckles in the opposite sense, this apparently requires the covalent adduct to trigger profound conformational changes in the protein or to buckle the FADH- opposite to that seen in the apo structure.

About this Structure

1V0J is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

Crystal structures of Mycobacteria tuberculosis and Klebsiella pneumoniae UDP-galactopyranose mutase in the oxidised state and Klebsiella pneumoniae UDP-galactopyranose mutase in the (active) reduced state., Beis K, Srikannathasan V, Liu H, Fullerton SW, Bamford VA, Sanders DA, Whitfield C, McNeil MR, Naismith JH, J Mol Biol. 2005 May 13;348(4):971-82. PMID:15843027

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