1ojr
From Proteopedia
(New page: 200px<br /> <applet load="1ojr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ojr, resolution 1.35Å" /> '''L-RHAMNULOSE-1-PHOS...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1OJR is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with ZN, PO4, 2HA, DIO and GOL as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.19 4.1.2.19]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OJR OCA]]. | + | 1OJR is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with ZN, PO4, 2HA, DIO and GOL as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Rhamnulose-1-phosphate_aldolase Rhamnulose-1-phosphate aldolase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.19 4.1.2.19]]. Structure known Active Site: ZN. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OJR OCA]]. |
==Reference== | ==Reference== | ||
Structure and catalytic mechanism of L-rhamnulose-1-phosphate aldolase., Kroemer M, Merkel I, Schulz GE, Biochemistry. 2003 Sep 16;42(36):10560-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12962479 12962479] | Structure and catalytic mechanism of L-rhamnulose-1-phosphate aldolase., Kroemer M, Merkel I, Schulz GE, Biochemistry. 2003 Sep 16;42(36):10560-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12962479 12962479] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| + | [[Category: Rhamnulose-1-phosphate aldolase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Kroemer, M.]] | [[Category: Kroemer, M.]] | ||
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[[Category: zinc enzyme]] | [[Category: zinc enzyme]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:26:13 2007'' |
Revision as of 10:21, 30 October 2007
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L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT E192A)
Overview
The structure of L-rhamnulose-1-phosphate aldolase has been established at, 1.35 A resolution in a crystal form that was obtained by a surface, mutation and has one subunit of the C(4)-symmetric tetramer in the, asymmetric unit. It confirms an earlier 2.7 A resolution structure which, was determined in a complicated crystal form with 20 subunits per, asymmetric unit. The chain fold and the active center are similar to those, of L-fuculose-1-phosphate aldolase and L-ribulose-5-phosphate 4-epimerase., The active center similarity is supported by a structural comparison of, all three enzymes and by the binding mode of the inhibitor, phosphoglycolohydroxamate at the site of the product dihydroxyacetone, phosphate for the two aldolases. The sensitivity of the catalytic rate to, several ... [(full description)]
About this Structure
1OJR is a [Single protein] structure of sequence from [Escherichia coli] with ZN, PO4, 2HA, DIO and GOL as [ligands]. Active as [Rhamnulose-1-phosphate aldolase], with EC number [4.1.2.19]. Structure known Active Site: ZN. Full crystallographic information is available from [OCA].
Reference
Structure and catalytic mechanism of L-rhamnulose-1-phosphate aldolase., Kroemer M, Merkel I, Schulz GE, Biochemistry. 2003 Sep 16;42(36):10560-8. PMID:12962479
Page seeded by OCA on Tue Oct 30 12:26:13 2007
Categories: Escherichia coli | Rhamnulose-1-phosphate aldolase | Single protein | Kroemer, M. | Merkel, I. | Schulz, G.E. | 2HA | DIO | GOL | PO4 | ZN | Aldolase (lyase) | Bacterial l-rhamnose metabolism | C4-tetramer | Class ii | Cleavage of l-rhamnulose-1-phosphate to dihydroxyacetonephosphate and l-lactaldehyde | Zinc enzyme
