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| - | [[Image:1mi3.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1mi3| PDB=1mi3 | SCENE= }} | | {{STRUCTURE_1mi3| PDB=1mi3 | SCENE= }} |
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| - | '''1.8 Angstrom structure of xylose reductase from Candida tenuis in complex with NADH'''
| + | ===1.8 Angstrom structure of xylose reductase from Candida tenuis in complex with NADH=== |
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| - | ==Overview==
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| - | The co-ordinates reported have been submitted to the Protein Data Bank under accession number 1MI3. Xylose reductase (XR; AKR2B5) is an unusual member of aldo-keto reductase superfamily, because it is one of the few able to efficiently utilize both NADPH and NADH as co-substrates in converting xylose into xylitol. In order to better understand the basis for this dual specificity, we have determined the crystal structure of XR from the yeast Candida tenuis in complex with NAD(+) to 1.80 A resolution (where 1 A=0.1 nm) with a crystallographic R -factor of 18.3%. A comparison of the NAD(+)- and the previously determined NADP(+)-bound forms of XR reveals that XR has the ability to change the conformation of two loops. To accommodate both the presence and absence of the 2'-phosphate, the enzyme is able to adopt different conformations for several different side chains on these loops, including Asn(276), which makes alternative hydrogen-bonding interactions with the adenosine ribose. Also critical is the presence of Glu(227) on a short rigid helix, which makes hydrogen bonds to both the 2'- and 3'-hydroxy groups of the adenosine ribose. In addition to changes in hydrogen-bonding of the adenosine, the ribose unmistakably adopts a 3'- endo conformation rather than the 2'- endo conformation seen in the NADP(+)-bound form. These results underscore the importance of tight adenosine binding for efficient use of either NADH or NADPH as a co-substrate in aldo-keto reductases. The dual specificity found in XR is also an important consideration in designing a high-flux xylose metabolic pathway, which may be improved with an enzyme specific for NADH. | + | The line below this paragraph, {{ABSTRACT_PUBMED_12733986}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12733986 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12733986}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Beta-alpha barrel]] | | [[Category: Beta-alpha barrel]] |
| | [[Category: Dimer]] | | [[Category: Dimer]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:05:19 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 00:01:11 2008'' |
Revision as of 21:01, 2 July 2008
Template:STRUCTURE 1mi3
1.8 Angstrom structure of xylose reductase from Candida tenuis in complex with NADH
Template:ABSTRACT PUBMED 12733986
About this Structure
1MI3 is a Single protein structure of sequence from Candida tenuis. Full crystallographic information is available from OCA.
Reference
Structure of xylose reductase bound to NAD+ and the basis for single and dual co-substrate specificity in family 2 aldo-keto reductases., Kavanagh KL, Klimacek M, Nidetzky B, Wilson DK, Biochem J. 2003 Jul 15;373(Pt 2):319-26. PMID:12733986
Page seeded by OCA on Thu Jul 3 00:01:11 2008
