1p4m: Difference between revisions

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[[Image:1p4m.~~jpg~~|left|200px]]

[[Image:1p4m.png|left|200px]]

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~~'''~~CRYSTAL STRUCTURE OF RIBOFLAVIN KINASE~~'''~~

===CRYSTAL STRUCTURE OF RIBOFLAVIN KINASE===

~~==Overview==~~

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~~Riboflavin kinase (RFK) is an essential enzyme catalyzing~~ the ~~phosphorylation of riboflavin (vitamin B(2))~~ to ~~form FMN, an obligatory step in vitamin B~~(~~2) utilization and flavin cofactor synthesis~~. ~~The structure of human RFK revealed a six-stranded antiparallel beta barrel core structurally similar to the riboflavin synthase/ferredoxin reductase FAD binding domain fold~~. ~~The binding site of an intrinsically bound MgADP defines a novel nucleotide binding motif that encompasses a loop, a 3(10~~) ~~helix~~, ~~and a reverse turn followed by a short beta strand. This active site loop forms an arch with ATP and riboflavin binding at~~ the ~~opposite side and the phosphoryl transfer appears to occur through the hole underneath the arch. The invariant residues Asn36 and Glu86 are implicated in the catalysis~~.

The line below this paragraph, {{ABSTRACT_PUBMED_12623014}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12623014 is the PubMed ID number.

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==About this Structure==

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[[Category: Flavin mononucleotide]]

[[Category: Riboflavin kinase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 04~~:40:54 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:56:44 2008''

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-[[Image:1p4m.jpg|left|200px]]
+{{Seed}}
+[[Image:1p4m.png|left|200px]]
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 {{STRUCTURE_1p4m|  PDB=1p4m  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF RIBOFLAVIN KINASE'''
+===CRYSTAL STRUCTURE OF RIBOFLAVIN KINASE===
-==Overview==
+<!--
-Riboflavin kinase (RFK) is an essential enzyme catalyzing the phosphorylation of riboflavin (vitamin B(2)) to form FMN, an obligatory step in vitamin B(2) utilization and flavin cofactor synthesis. The structure of human RFK revealed a six-stranded antiparallel beta barrel core structurally similar to the riboflavin synthase/ferredoxin reductase FAD binding domain fold. The binding site of an intrinsically bound MgADP defines a novel nucleotide binding motif that encompasses a loop, a 3(10) helix, and a reverse turn followed by a short beta strand. This active site loop forms an arch with ATP and riboflavin binding at the opposite side and the phosphoryl transfer appears to occur through the hole underneath the arch. The invariant residues Asn36 and Glu86 are implicated in the catalysis.
+The line below this paragraph, {{ABSTRACT_PUBMED_12623014}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12623014 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12623014}}
 ==About this Structure==
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 [[Category: Flavin mononucleotide]]
 [[Category: Riboflavin kinase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:40:54 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:56:44 2008''