1nzc: Difference between revisions

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[[Image:1nzc.jpg|left|200px]]<br /><applet load="1nzc" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1nzc.jpg|left|200px]]
caption="1nzc, resolution 1.80&Aring;" />
 
'''The high resolution structures of RmlC from Streptococcus suis in complex with dTDP-D-xylose'''<br />
{{Structure
|PDB= 1nzc |SIZE=350|CAPTION= <scene name='initialview01'>1nzc</scene>, resolution 1.80&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene> and <scene name='pdbligand=TDX:THYMIDINE-5'-DIPHOSPHO-BETA-D-XYLOSE'>TDX</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/dTDP-4-dehydrorhamnose_3,5-epimerase dTDP-4-dehydrorhamnose 3,5-epimerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.3.13 5.1.3.13]
|GENE= rmlc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1307 Streptococcus suis])
}}
 
'''The high resolution structures of RmlC from Streptococcus suis in complex with dTDP-D-xylose'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1NZC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_suis Streptococcus suis] with <scene name='pdbligand=NI:'>NI</scene> and <scene name='pdbligand=TDX:'>TDX</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/dTDP-4-dehydrorhamnose_3,5-epimerase dTDP-4-dehydrorhamnose 3,5-epimerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.3.13 5.1.3.13] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NZC OCA].  
1NZC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_suis Streptococcus suis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NZC OCA].  


==Reference==
==Reference==
High-resolution structures of RmlC from Streptococcus suis in complex with substrate analogs locate the active site of this class of enzyme., Dong C, Major LL, Allen A, Blankenfeldt W, Maskell D, Naismith JH, Structure. 2003 Jun;11(6):715-23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12791259 12791259]
High-resolution structures of RmlC from Streptococcus suis in complex with substrate analogs locate the active site of this class of enzyme., Dong C, Major LL, Allen A, Blankenfeldt W, Maskell D, Naismith JH, Structure. 2003 Jun;11(6):715-23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12791259 12791259]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Streptococcus suis]]
[[Category: Streptococcus suis]]
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[[Category: jelly roll-like structure; beta sheet]]
[[Category: jelly roll-like structure; beta sheet]]


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Revision as of 14:03, 20 March 2008

File:1nzc.jpg


PDB ID 1nzc

Drag the structure with the mouse to rotate
, resolution 1.80Å
Ligands: and
Gene: rmlc (Streptococcus suis)
Activity: dTDP-4-dehydrorhamnose 3,5-epimerase, with EC number 5.1.3.13
Coordinates: save as pdb, mmCIF, xml



The high resolution structures of RmlC from Streptococcus suis in complex with dTDP-D-xylose


OverviewOverview

Nature achieves the epimerization of carbohydrates by a variety of chemical routes. One common route is that performed by the class of enzyme defined by dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase (RmlC) from the rhamnose pathway. Earlier studies failed to identify the key residues in catalysis. We report the 1.3 A structure of RmlC from Streptococcus suis type 2 and its complexes with dTDP-D-glucose and dTDP-D-xylose. The streptococcal RmlC enzymes belong to a separate subgroup, sharing only 25% identity with RmlC from other bacteria, yet the S. suis enzyme has similar kinetic properties and structure to other RmlC enzymes. Structure, sequence alignment, and mutational analysis have now allowed reliable identification of the catalytic residues and their roles.

About this StructureAbout this Structure

1NZC is a Single protein structure of sequence from Streptococcus suis. Full crystallographic information is available from OCA.

ReferenceReference

High-resolution structures of RmlC from Streptococcus suis in complex with substrate analogs locate the active site of this class of enzyme., Dong C, Major LL, Allen A, Blankenfeldt W, Maskell D, Naismith JH, Structure. 2003 Jun;11(6):715-23. PMID:12791259

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