From Proteopedia
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| - | [[Image:1i10.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} | | {{STRUCTURE_1i10| PDB=1i10 | SCENE= }} |
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| - | '''HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE'''
| + | ===HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE=== |
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| - | ==Overview==
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| - | Lactate dehydrogenase (LDH) interconverts pyruvate and lactate with concomitant interconversion of NADH and NAD(+). Although crystal structures of a variety of LDH have previously been described, a notable absence has been any of the three known human forms of this glycolytic enzyme. We have now determined the crystal structures of two isoforms of human LDH-the M form, predominantly found in muscle; and the H form, found mainly in cardiac muscle. Both structures have been crystallized as ternary complexes in the presence of the NADH cofactor and oxamate, a substrate-like inhibitor. Although each of these isoforms has different kinetic properties, the domain structure, subunit association, and active-site regions are indistinguishable between the two structures. The pK(a) that governs the K(M) for pyruvate for the two isozymes is found to differ by about 0.94 pH units, consistent with variation in pK(a) of the active-site histidine. The close similarity of these crystal structures suggests the distinctive activity of these enzyme isoforms is likely to result directly from variation of charged surface residues peripheral to the active site, a hypothesis supported by electrostatic calculations based on each structure. Proteins 2001;43:175-185.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11276087}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11276087 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11276087}} |
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| | ==Disease== | | ==Disease== |
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| | [[Category: Dehydrogenase]] | | [[Category: Dehydrogenase]] |
| | [[Category: Rossman fold]] | | [[Category: Rossman fold]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:26:47 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:15:00 2008'' |
Revision as of 07:15, 1 July 2008
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| 1i10, resolution 2.30Å ()
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| Ligands:
| , ,
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| Gene:
| LDHA (Homo sapiens)
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| Activity:
| L-lactate dehydrogenase, with EC number 1.1.1.27
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| Related:
| 1i0z, 9ldt, 5ldh, 1ldg
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| Structural annotation:
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| Resources:
| CATH : 1I10A02, 1I10A01, 1I10B01, 1I10B02, 1I10C02, 1I10C01, 1I10D01, 1I10D02, 1I10E02, 1I10E01, 1I10F01, 1I10F02, 1I10G02, 1I10G01, 1I10H01, 1I10H02
InterPro : Ipr001557, Ipr001236, Ipr011304
Pfam : PF00056, PF02866
SCOP : d1i10a1, d1i10a2, d1i10b2, d1i10b1, d1i10c2, d1i10c1, d1i10d1, d1i10d2, d1i10e1, d1i10e2, d1i10f1, d1i10f2, d1i10g2, d1i10g1, d1i10h2, d1i10h1
UniProt : P00338
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| Resources:
| FirstGlance, OCA, RCSB, PDBsum
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| Coordinates:
| save as pdb, mmCIF, xml
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HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE
Template:ABSTRACT PUBMED 11276087
Disease
Known disease associated with this structure: Exertional myoglobinuria due to deficiency of LDH-A OMIM:[150000]
About this Structure
1I10 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural basis for altered activity of M- and H-isozyme forms of human lactate dehydrogenase., Read JA, Winter VJ, Eszes CM, Sessions RB, Brady RL, Proteins. 2001 May 1;43(2):175-85. PMID:11276087
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